1

Amino Acids WS
1 [M’16 P42 Q9]
19

(c)

amino acid formula

T CH3CH(NH2)CO2H

U C6H5CH2CH(NH2)CO2H

V H2N(CH2)4CH(NH2)CO2H

(i) Which of the amino acids T, U or V has the highest pH in aqueous solution? Explain why.

amino acid ..............................

.............................................................................................................................................

.............................................................................................................................................
[1]

(ii) State how many different dipeptides could be formed from a reaction mixture consisting of
amino acids T and U.

....................................................................................................................................... [1]

(iii) Polypeptides contain a high proportion of carbon and hydrogen in their structures, yet
many are soluble in water.

By referring to the structure of a polypeptide, explain why.

.............................................................................................................................................

.............................................................................................................................................

.............................................................................................................................................

....................................................................................................................................... [2]

[Total: 10]

Bilal Hameed Amino Acids

[Turn over
© UCLES 2016 9701/42/F/M/16
 ....................................................................................................................................... [1]

(ii) State the mathematical relationship between

2 pKa and the acidity constant Ka.

.......................................................................................................................................
14 [1]
2 [S’17 P42 Q6]

6 The (iii)
tableGive
lists reasons for whyacids
some organic the pKa value
and theirfor
pKchloroethanoic
a values.
acid is smaller than that for ethanoic
acid.
acid formula pKa
.............................................................................................................................................
ethanoic acid CH3CO2H 4.76
.............................................................................................................................................
chloroethanoic acid Cl CH2CO2H 2.86
....................................................................................................................................... [2]
aminoethanoic acid (glycine) H2NCH2CO2H 9.87

(a) (i) State the relationship between pKa and the strength of an acid.
(b) (i) Use the zwitterionic structure for aminoethanoic acid (glycine) in aqueous solution to write
an equation for its dissociation giving H+(aq) ions.
....................................................................................................................................... [1]
....................................................................................................................................... [1]
(ii) State the mathematical relationship between pKa and the acidity constant Ka.
(ii) Calculate the pH of a 0.100 mol dm–3 solution of aminoethanoic acid.
....................................................................................................................................... [1]

(iii) Give reasons for why the pKa value for chloroethanoic acid is smaller than that for ethanoic
3 [W’18 P41acid.
Q6]
15

6 (a) Use .............................................................................................................................................

the Data Booklet to draw the structure of the dipeptide val-lys. The peptide bond should
be shown displayed.
.............................................................................................................................................

....................................................................................................................................... [2]

(b) (i) Use the zwitterionic structure for aminoethanoic acid (glycine) in aqueous solution to write
an equation for its dissociation giving H+(aq) ions.
pH = .............................. [2]
....................................................................................................................................... [1]

(ii) Calculate the pH of a 0.100 mol dm–3 solution of aminoethanoic acid. [2]

(b) The isoelectric point is the pH at which an amino acid exists as a zwitterion. The isoelectric

A mixture of the dipeptide, val-lys, and its two constituent amino acids, valine and lysine, was
© UCLES 2017 9701/42/M/J/17

Draw and label three spots on the diagram of the electrophoresis paper to indicate the likely
position of each of these three species after electrophoresis. Explain your answer.

+ –
pH = .............................. [2]

mixture applied here

explanation .........................................................................................................................

.............................................................................................................................................

.............................................................................................................................................
© UCLES 2017 9701/42/M/J/17 [5]
Amino Acids Bilal Hameed
[Total: 7]
 3

4 [W’17 P42 Q3]

6

3 Serotonin can be synthesised from the amino acid tryptophan in two steps.

NH2 NH2
HO
CO2H CO2H

N N
H H
tryptophan

NH2
HO

N
H
serotonin

(a) (i) In a buffer solution at pH 5.9, a sample of tryptophan does not move during electrophoresis.

Draw the structures of the ions formed by tryptophan at pH 1.0 and pH 5.9.

pH 1.0 pH 5.9
[2]

(ii) Tryptophan can combine with valine to form a dipeptide.

Use the Data Booklet to draw the structure of this dipeptide.

[2]

© UCLES 2017 9701/42/O/N/17

Bilal Hameed Amino Acids

 4

5 [S’18 P42 Q7]

12

7 Asparagine and valine are two naturally occurring amino acids.

O O
O
OH OH
NH2 NH2 NH2

asparagine valine

(a) Give the molecular formula of asparagine.

.............................................................................................................................................. [1]

(b) Name all of the functional groups in an asparagine molecule.

.............................................................................................................................................. [2]

(c) Draw the structure of the dipeptide formed by valine and asparagine.

The peptide bond should be shown displayed and should be clearly labelled.

[2]

(d) A solution of valine in water acts as a buffer solution.

(i) Explain what is meant by a buffer solution.

.............................................................................................................................................

.............................................................................................................................................

....................................................................................................................................... [2]

(ii) Write two equations to explain how valine can act as a buffer. Use the formula H2NCHRCO2H
for valine in your equations.

.............................................................................................................................................

.............................................................................................................................................
[2]

© UCLES 2018 9701/42/M/J/18

Amino Acids Bilal Hameed

 5
13

(e) Each valine molecule has one chiral carbon atom.

Draw three-dimensional diagrams to show the two optical isomers of valine.

The (CH3)2CH group can be represented as R.

[2]

(f) Asparagine is hydrolysed when heated with aqueous sulfuric acid.

Write an equation for this reaction.

.............................................................................................................................................. [2]

[Total: 13]

© UCLES 2018 9701/42/M/J/18 [Turn over

Bilal Hameed Amino Acids

:
B
R
-
r
6 [S’19 P42 Q7]
(b)

(i)
.............................................................................................................................................

.............................................................................................................................................

2
2

2
2

CO2
CO2

l
6
....................................................................................................................................... [1]

......................................................................................

2 2 CO2 ...................................................................................
[2]

20

(ii)

© UCLES 2019 9701/42/M/J/19 [Turn over

.............................................................................................................................................

.............................................................................................................................................

.............................................................................................................................................
[2]

(c)
stereoisomerism.

3 2 )CO2

C C

I
-
E
[1]

§ (d) 3 l CO2

(i)

.....................................................................................................

...........................................................................................................
[2]

(ii)
ethanoic acid.

.............................................................................................................................................

.............................................................................................................................................

Amino Acids Bilal Hameed

.............................................................................................................................................

.............................................................................................................................................
 .....................................................................................................

...........................................................................................................
7 [2]

(ii)
ethanoic acid.

.............................................................................................................................................

.............................................................................................................................................

.............................................................................................................................................

.............................................................................................................................................

.......................................................................................................................................
21 [3]

(e) 2 2 )CO2 3 2)CO2

© UCLES 2019 structural 9701/42/M/J/19 6 12 2 O4.

6 12 2 O4) 6 12 2 O4)

6 12 2 O4)

[3]

[Total: 15]

Bilal Hameed Amino Acids

; State two different processes by which some polymers can be degraded.

....................................................................................................................................................
8
.............................................................................................................................................. [1]
7 [S’20 P42 Q6]
(e) The cyclic peptide B is shown.

O
O

N
H HN

O NH O
O
S HN
-

E NH
HN
D H O
O N

HO O

Cyclic peptide B
The amino acid threonine, Thr, and two other organic products are formed.

threonine
OH

H2N CO2H

© UCLES 2020 9701/42/M/J/20

Amino Acids Bilal Hameed

 9
19

(i) Draw the structures of the two other organic products formed.

[2]

(ii) Using the 3-letter abbreviations for the amino acids as given in the Data Booklet, complete
the sequence for the cyclic peptide, B.

..................

.................. ..................

± .................. ..................

Thr ..................
[1]

(iii) Name two analytical techniques that could be used to separate these amino acids.

................................................................ and ............................................................. [1]

[Total: 12]

© UCLES 2020 9701/42/M/J/20 [Turn over

Bilal Hameed Amino Acids

 10

Electrophoresis
PAGE 147
WS 1
1 [J’16 P41 Q7]
10

10
7 (a) (i) Use the Data Booklet to draw the structure of the tripeptide Ala-Ser-Gly showing its peptide
bonds in full.

Ala-Ser-Gly
[2]

(ii) Calculate the relative molecular mass, Mr, of Ala-Ser-Gly.

Mr = ............................ [1]

(b) Electrophoresis can be used to separate mixtures of amino acids and peptides.
A mixture of the tripeptide Ala-Ser-Gly and its three constituent amino acids was subjected to
electrophoresis in a buffer at pH 11.

(i) Draw the structure of serine at pH 11.

[1]

Electrophoresis
© UCLES 2016 1 9701/41/M/J/16 Bilal Hameed
 PAGE 148
11
11

At the end of the experiment the following results were seen.

mixture
applied here

G H
P Q R S I

(ii) Identify the components labelled F-I in the above diagram.

F .........................................................................................................................................

G .........................................................................................................................................

H .........................................................................................................................................

I ..........................................................................................................................................
[4]

(iii) Suggest the identities of the species responsible for

spot P, ................................................................................................................................

spot S. ................................................................................................................................

Explain your answers.

.............................................................................................................................................

....................................................................................................................................... [3]

(c) (i) State the reagents and conditions needed for converting the tripeptide into its three
constituent amino acids.

....................................................................................................................................... [1]

(ii) Name the type of reaction in (i).

....................................................................................................................................... [1]

[Total: 13]

© UCLES 2016 9701/41/M/J/16 [Turn over

CEDAR COLLEGE
Bilal Hameed ELECTROPHORESIS WS 1 1
Electrophoresis
 12
PAGE 149
2 [J’16 P41 Q7]
14

11
7 (a) Amino acids can be separated by electrophoresis.

(i) Draw a labelled diagram of the apparatus used to separate a mixture by electrophoresis.

[3]

(ii) Explain the principles of the separation of amino acids by electrophoresis.

.............................................................................................................................................

.............................................................................................................................................

....................................................................................................................................... [2]

(b) Electrophoresis is usually carried out in a buffer solution.

Given three buffers, with pH values of 2.0, 7.0 and 12.0, suggest, with a reason, which buffer
would be the most suitable for the separation of the following amino acid mixtures.
Your reasons should refer to the structure of each molecule.
(The structures of these amino acids are given in the Data Booklet.)

(i) Asp and Val

buffer pH .............................................................................................................................

reason .................................................................................................................................

.............................................................................................................................................

(ii) Lys and Ser

buffer pH .............................................................................................................................

reason .................................................................................................................................

.............................................................................................................................................

(iii) Tyr and Phe

buffer pH .............................................................................................................................

reason .................................................................................................................................

.............................................................................................................................................
[3]

© UCLES 2016 9701/42/M/J/16

Electrophoresis 1 Bilal Hameed

CEDAR COLLEGE ELECTROPHORESIS WS 1
 PAGE 150
13
15

(c) (i) Draw the structure of the dipeptide Gly-Ser, showing the peptide bond in full.

[2]

The infra-red spectrum of Gly-Ser is shown below.

100
transmittance

50

E
G
F
0
4000 3000 2000 1500 1000 500
wavenumber / cm –1

(ii) Use the Data Booklet to identify the bond in the molecule of Gly-Ser that is responsible for
each of the peaks indicated on the above infra-red spectrum.

E ............................................

F ............................................

G ............................................
[2]

[Total: 12]

© UCLES 2016 9701/42/M/J/16 [Turn over

Bilal Hameed
CEDAR COLLEGE Electrophoresis
ELECTROPHORESIS WS 1 1
 14

3 [J’17 P42 Q8]

20

(b) The dipeptide phe-tyr has the following structure.

H
N CO2H
H 2N
O

OH

A mixture of this dipeptide (phe-tyr) and its two constituent amino acids (phe and tyr) was
subjected to electrophoresis in a buffer at pH 12. At the end of the experiment the following
results were seen. Spots R and S remained very close together.

mixture applied here

+ –

P R S

The three spots are due to the three species phe, tyr and phe-tyr.

(i) Which species is responsible for spot P? Explain your answer.

.............................................................................................................................................

....................................................................................................................................... [2]

(ii) Suggest why the other two species give spots R and S that are so close together.

.............................................................................................................................................

....................................................................................................................................... [1]

[Total: 15]

Permission to reproduce items where third-party owned material protected by copyright is included has been sought and cleared where possible. Every reasonable
effort has been made by the publisher (UCLES) to trace copyright holders, but if any items requiring clearance have unwittingly been included, the publisher will
be pleased to make amends at the earliest possible opportunity.

To avoid the issue of disclosure of answer-related information to candidates, all copyright acknowledgements are reproduced online in the Cambridge International
Examinations Copyright Acknowledgements Booklet. This is produced for each series of examinations and is freely available to download at www.cie.org.uk after
the live examination series.

Cambridge International Examinations is part of the Cambridge Assessment Group. Cambridge Assessment is the brand name of University of Cambridge Local
Examinations Syndicate (UCLES), which is itself a department of the University of Cambridge.

© UCLES 2017 9701/42/M/J/17

Electrophoresis 1 Bilal Hameed

 15

4 [N’17 P42 Q3]

6

3 Serotonin can be synthesised from the amino acid tryptophan in two steps.

NH2 NH2
HO
CO2H CO2H

N N
H H
tryptophan

NH2
HO

N
H
serotonin

(a) (i) In a buffer solution at pH 5.9, a sample of tryptophan does not move during electrophoresis.

Draw the structures of the ions formed by tryptophan at pH 1.0 and pH 5.9.

pH 1.0 pH 5.9
[2]

(ii) Tryptophan can combine with valine to form a dipeptide.

Use the Data Booklet to draw the structure of this dipeptide.

[2]

© UCLES 2017 9701/42/O/N/17

Bilal Hameed Electrophoresis 1

 16
7

(b) Complete the following table to show the structures of the products formed and the
type of reaction occurring when serotonin reacts with the four reagents in separate reactions.

reagent structure of product type of reaction

Na

excess Br2(aq)

excess CH3COCl

excess H2 / Pt catalyst

[8]

© UCLES 2017 9701/42/O/N/17 [Turn over

Electrophoresis 1 Bilal Hameed

 17

5 [N’18 P41 Q6]

15

6 (a) Use the Data Booklet to draw the structure of the dipeptide val-lys. The peptide bond should
be shown displayed.

[2]

(b) The isoelectric point is the pH at which an amino acid exists as a zwitterion. The isoelectric
point o aline is . and o l sine is . .

A mixture of the dipeptide, val-lys, and its two constituent amino acids, valine and lysine, was
anal sed electrop oresis using a u er at p . .

Draw and label three spots on the diagram of the electrophoresis paper to indicate the likely
position of each of these three species after electrophoresis. Explain your answer.

+ –

mixture applied here

explanation .........................................................................................................................

.............................................................................................................................................

.............................................................................................................................................
[5]

[Total: 7]

© UCLES 2018 9701/41/O/N/18 [Turn over

Bilal Hameed Electrophoresis 1

 18

6 [N’18 P42 Q9]

23

9 (a) Use information from the Data Booklet to draw the structure of the dipeptide glu-cys.

[2]

The isoelectric point is the pH at which an amino acid exists as a zwitterion. The isoelectric point of
glutamic acid is 3.2 and of cysteine is 5.0.

A mixture of the dipeptide glu-cys and its two constituent amino acids, glutamic acid and cysteine,
was analysed by electrophoresis using a buffer at pH 5.2. The results obtained are shown.

+ –

E F G mixture applied here

(b) Suggest identities for the species responsible for spots E, F and G. Explain your answers.

spot identity

explanation ................................................................................................................................

....................................................................................................................................................

....................................................................................................................................................
[3]

[Total: 5]

© UCLES 2018 9701/42/O/N/18 [Turn over

Electrophoresis 1 Bilal Hameed

 PAGE16
141 For
Examiner’s
Use
9 Much of the preparation of evidence to solve PAGEcrimes
16141 now relies on instrumental analysis. This For
question deals with someELECTROPHORESISof the techniques used. 19 WS 1 Examiner’s
Use
9 Much of the preparation of evidence to solve crimes now relies on instrumental analysis. This
1question
(a) Electrophoresis
deals with can some Electrophoresis
ELECTROPHORESISWS
beofused WS 2
1
to separate used.
the techniques amino acids produced by hydrolysing proteins.
The amino acids are placed in a buffered solution in an electric field. In a solution of
1 given
1(a) pH, what two
Electrophoresis can factors
be used affect the movement
to separate aminoofacids a given amino by
produced acid?
hydrolysing proteins.
The amino acids are placed in a buffered solution in an electric field. In a solution of
(i)given
..................................................................................................................................
pH, what two factors affect the movement of a given amino acid?

(ii)(i) ..................................................................................................................................
..................................................................................................................................
[2]
(ii) ..................................................................................................................................
(b) Nuclear magnetic resonance (NMR) spectroscopy 14 and mass spectrometry are also used[2]
in the detection of certain molecules, particularly those containing hydrogen atoms.
3(b)The
72 Nuclear
analysis magnetic
of a proteinresonance
may be(NMR) carriedspectroscopy
out14 by breaking and it mass spectrometry
down into are also
its amino acids. used
These
For
Examiner’s
(i)in then
can Explain
the detectionhowofand
be separated bywhy
certain the NMR
molecules,
a process called spectrum
particularly ofthose
electrophoresis. propanal, CH3CH
containing CHO,
hydrogen
2 would
atoms. be Use
different from that of propanone,
73 The analysis of a protein may be carried out CH COCH ,
3 by breaking
3 which contains the same atoms.
it down into its amino acids. These
For
Examiner’
(a) (i)The
can structures
Explain
then howofand
be separated glycine,
bywhy lysine
the NMR
a process and
calledglutamic
spectrum acidofatpropanal,
electrophoresis. pH 7 are shown.
CH3CH2CHO, would be Use
..................................................................................................................................
different from that of propanone, CH3COCH3, which contains the same atoms.
(a) The glycine
structures of glycine, H3N+lysine
CH2CO and2
–
glutamic acid at pH 7 are shown.
..................................................................................................................................
..................................................................................................................................
lysine
glycine HH3N CH(CH2CH
+ + – CH CH NH +)CO –
3N CH2CO 2 2 2 2 3 2
..................................................................................................................................
..................................................................................................................................
glutamic
lysine acid HH3NN
+
CH(CH
CH(CH 2CH 2CO2 )CO2
– –
2CH2CH2CH2NH3 )CO2
+ + –
3
..................................................................................................................................
..................................................................................................................................
Drawglutamic
and label acidthree circlesH3N+on the chart
CH(CH below – to indicate the likely position of each of
2CH2CO2 )CO2
–

these amino acids after electrophoresis of a solution containing these amino acids in a
..................................................................................................................................
..................................................................................................................................
buffer at pH 7.
Draw and label three circles on the chart below to indicate the likely position of each of
(ii) Explain
these how acids
amino and why afterthe mass spectrum
electrophoresis of a of the two
solution compounds
containing theseinamino(i) would
acidsbe in a
..................................................................................................................................
different.
buffer at pH 7.
(ii) Explain how and why the mass spectrum of the two compounds in (i) would be
..................................................................................................................................
different.

..................................................................................................................................
start point
..................................................................................................................................

..................................................................................................................................
..................................................................................................................................
start point [3]

(b) Some..................................................................................................................................
..................................................................................................................................
organic compounds have very different solubilities in water and in organic solvents[3]
such as hexane. They may be extracted from an aqueous reaction mixture by shaking
..................................................................................................................................
(b) the mixture withcompounds
portions of hexane and separating the twoinlayers.
..................................................................................................................................
Some organic have very different solubilities water and in organic solvents
The process of distribution of a compound between two solvents is called partition. [4]
such as hexane. They may be extracted from an aqueous reaction mixture by shaking
the..................................................................................................................................
mixture with portions of hexane and separating the two layers.
(i)TheState
processwhatofisdistribution
meant by the of aterm partitionbetween
compound coefficient. two solvents is called partition. [4]

(i) ....................................................................................................................................
State what is meant by the term partition coefficient.
....................................................................................................................................
....................................................................................................................................
....................................................................................................................................
....................................................................................................................................
(ii) One of the concerns about organic pollutants, such as pesticide residues, is that they
....................................................................................................................................
can enter the food chain and become concentrated in human breast milk. Explain
(ii) how
Onethis canconcerns
of the happen. about organic pollutants, such as pesticide residues, is that they
can enter the food chain and become concentrated in human breast milk. Explain
....................................................................................................................................
how this can happen.
....................................................................................................................................
CEDAR COLLEGE ELECTROPHORESIS WS 1
....................................................................................................................................
© UCLES 2008 9701/04/M/J/08

Bilal
CEDAR Hameed ....................................................................................................................................
COLLEGE ELECTROPHORESIS Electrophoresis WS21
....................................................................................................................................
© UCLES 2008 9701/04/M/J/08
....................................................................................................................................
....................................................................................................................................
[3]
 PAGE 142
20 For
14
Examiner’s
Use
843 (a) Electrophoresis can be used to separate amino acids which are produced by the
hydrolysis of a polypeptide.

Using glycine as an example, explain why the result of electrophoresis depends on pH.

..........................................................................................................................................

..........................................................................................................................................

..........................................................................................................................................

......................................................................................................................................[3]

(b) The diagram below shows the results of electrophoresis in neutral solution. At the start
of the experiment a spot of a solution containing a mixture of amino acids P, Q, R and S
was placed in the middle of the plate. Following electrophoresis the amino acids had
moved to the positions shown in the lower diagram.

before + –

after + –

P Q R S

(i) Which amino acid existed mainly as a zwitterion in the buffer solution?
Explain your answer.

..................................................................................................................................

..................................................................................................................................

(ii) Assuming amino acids R and S carry the same charge when in this buffer solution,
which is likely to be the larger molecule? Explain your answer.

..................................................................................................................................

..................................................................................................................................
[2]

(c) Amino acids may also be separated by using two-dimensional paper chromatography.
This involves putting a spot of the mixture on the corner of a piece of chromatography
paper and allowing a solvent to soak up the paper. The paper is then dried, turned
through 90° and placed in a second solvent. This method gives better separation than a
one solvent method.

(i) Paper chromatography relies on partition between the solvent applied and another
phase.

What is this second phase? .......................................................

© UCLES 2007 9701/04/M/J/07

Electrophoresis
CEDAR COLLEGE 2 Bilal Hameed
ELECTROPHORESIS WS 1
 PAGE 143
2114

5
74 A mixture of amino acids may be separated using electrophoresis. A typical practical set-up For
is shown in the diagram. Examiner’s
Use

d.c. power supply

+ –
electrolyte glass slides

amino acid mixture placed here filter paper soaked in buffer solution

(a) When the power supply is switched on, some amino acids may not move, but remain
stationary. Suggest an explanation for this observation.

..........................................................................................................................................

..........................................................................................................................................

...................................................................................................................................... [2]

(b) The amino acid glycine has the formula H2NCH2CO2H. Identify the species formed on
the filter paper if glycine moves to the left (positive) end of the filter paper.

.................................................................. [1]

(c) The following result was obtained from another electrophoresis. What can be deduced
about the relative sizes of, and charges on, the amino acid species A, B and C?

+ –

A B C
mixture placed here

amino acid relative size charge

[3]

© UCLES 2010 9701/42/M/J/10

Bilal Hameed
CEDAR COLLEGE Electrophoresis
ELECTROPHORESIS WS 1 2
 PAGE 144
2215

(d) The sequence of amino acids in a polypeptide

16 may be determined by partial hydrolysis For
of the chain into smaller pieces, often tripeptides. Examiner’s
Use
7 Modern methods of chemical analysis often rely on the interpretation of data gathered from
(i) Following
instrumental such a partial hydrolysis, the following tripeptides were obtained from a
techniques.
given polypeptide.
(a) Electrophoresis and paper chromatography can both be used to separate amino acids from a
mixture obtained fromgly-ala-gly
ala-gly-asp polypeptides. lys-val-ser ser-ala-gly val-ser-ala

d.c.that
Given the N-terminal amino acid is lysine (lys)lidsuggest the amino acid sequence
power
supply
of the shortest polypeptide
glass slidesthat would give the above tripeptides.
+ –
..................................................................................................................................
paper solvent
The structural formulae of the amino acids in the polypeptide are given below.
front

mixtures placed
abbreviation amino acid structural formula here
amino acid ala filter paper soaked
alanine H2NCH(CH3)CO2H solvent
mixture placed here in buffer solution
asp aspartic acid H2NCH(CH2CO2H)CO2H
electrophoresis paper chromatography
gly glycine H2NCH2CO2H
In each case, give one property of the amino acids that causes their separation.
lys lysine H2NCH(CH2CH2CH2CH2NH2)CO2H
electrophoresis
ser ..........................................................................................................................
serine H NCH(CH OH)CO H
2 2 2
....................................................................................................................................................
val valine H NCH(CH(CH ) )CO H
2 3 2 2

paper chromatography ..............................................................................................................

(ii) Which of the tripeptides in (i) has the lowest Mr?
....................................................................................................................................................
.......................................................................... [2]

(b) (iii)
AminoSelect
acids are
onecolourless.
amino acid from those listed in the table which contains an ionic
side-chain at pH 8.
How are the positions of the different amino acids made visible so that measurements can be
made?
..........................................................................
....................................................................................................................................................
[4]
.............................................................................................................................................. [1]
[Total: 10]

6 (c) Which measurements need to be made in order to identify individual amino acids in paper
chromatography?

....................................................................................................................................................

.............................................................................................................................................. [1]

© UCLES 2014 9701/42/M/J/14

© UCLES 2010 9701/42/M/J/10 [Turn over

CEDAR COLLEGE ELECTROPHORESIS WS 1
Electrophoresis 2 Bilal Hameed
 PAGE
PAGE145
145
23
1717

5 (d)(d)The
Thediagram
diagramshows
showsthethe
results of of
results 1414 onon
electrophoresis
electrophoresis a mixture of of
a mixture thethe
amino acids
amino glycine,
acids glycine,
lysine and glutamic acid at pH 7.0. The structures of the amino acids at pH 7.0 are shown.
lysine and glutamic acid at pH 7.0. The structures of the amino acids at pH 7.0 are shown.
7 7 One
Oneof of
thethe
key areas
key of of
areas investigation in in
investigation understanding
understanding thethe
structures of of
structures polypeptides and
polypeptides and For For
glycine:
glycine:
proteins is is
proteins thethe N3+N
H3H
sequence
sequenceCH+ CO – –
ofCH
of 2CO
amino2 2acids
2 amino that
acids make
that up
make the
up polypeptide
the polypeptidechains.
chains. Examiner’s
Examiner’s
lysine:
lysine: +
H3H
N3NCH(CH
+
CH(CH 2CH 2CH
2CH 2CH
2CH 2NH
+
2CH 3 )CO
–
2NH 3 )CO
+
2 2
–
UseUse

(a)(a)glutamic acid: H3H

N3NCH(CH to2CH 2CO 2 )CO
+ + – – – –
glutamic
OneOneof of
the acid:
methods
the methods CH(CH
used
used 2CH 2CO
determine
to 2 )CO
determine the
2 2amino acids present in a polypeptide chain is
the amino acids present in a polypeptide chain is
electrophoresis.
electrophoresis.
+ + – –
Sketch and
Sketch label
and thethe
label apparatus used
apparatus to to
used carry outout
carry electrophoresis.
electrophoresis.

spot of of
spot mixture
mixture
applied
appliedhere
here

+ + – –

RR SS T T

Identify thethe
Identify amino acids
amino responsible
acids forfor
responsible thethe
spots labelled
spots R,R,
labelled S and T. T.
S and

RR
................................................................................................................................................
................................................................................................................................................

SS
................................................................................................................................................
................................................................................................................................................

T T
................................................................................................................................................
................................................................................................................................................
[4]
[3][4]
[3]

6 7(b)
7 (e)(b)InThis
electrophoresis,
(e)This
In diagram shows different
the
electrophoresis,
diagram shows results
different
the amino
of amino
results of acids
two-way move
paper
acids
two-way move
paper in in
different
chromatography directions
different
chromatography of and
ofdirections
a mixture of
a mixture atamino
different
amino
and
of at acids.
different
acids.
speeds.
speeds.

(i) (i) What

Whatfactors determine
factors thethe
determine direction of of
direction travel of of
travel anan
amino acid?
amino acid?

..................................................................................................................................
..................................................................................................................................

..................................................................................................................................
..................................................................................................................................
solvent 1 1
solvent
..................................................................................................................................
..................................................................................................................................

(ii)(ii) What
Whatfactors determine
factors thethe
determine speed of of
speed movement of of
movement anan
amino acid?
amino acid?
mixture
mixture XX
..................................................................................................................................
applied here
..................................................................................................................................
applied here solvent 2
solvent 2
..................................................................................................................................
..................................................................................................................................
ToToanswer
answer these
these questions
questions youyouneedneed to to
indicate
indicate clearly
clearly ononthethediagram
diagram above
above asas directed
directed in in
[3][3]
thethe
questions.
questions.
(i) (i)PutPut
aU a next to to
U next thethe
amino acid
amino that
acid travelled
that furthest
travelled in in
furthest solvent 2. 2.
solvent
(ii)(ii)PutPut
a ring around
a ring thethe
around two amino
two acids
amino that
acids were
that not
were separated
not in in
separated solvent 1. 1.
solvent
(iii)(iii)PutPut
aW next
aW to to
next thethe
amino acid
amino that
acid was
that very
was soluble
very in in
soluble both solvents.
both solvents.
[3][3]

[Total: 10]10]
[Total:

© UCLES 2014
© UCLES 2014 9701/42/M/J/14
9701/42/M/J/14
[Turn over
[Turn over

Bilal
CEDAR
CEDARHameed
COLLEGE
COLLEGE
© UCLES 2011 9701/42/O/N/11
Electrophoresis
ELECTROPHORESIS
ELECTROPHORESIS WS WS 12 1
© UCLES 2011 9701/42/O/N/11
 PAGE 146
[4]
PAGE 146
24 [4]
8 (b) How far an amino acid will travel during electrophoresis depends on the pH of the solution.
For a given potential difference, state two other factors that will affect how far a given
8
7 (b) How far an amino acid will travel during electrophoresis depends on the pH of the solution.
amino acid travels in a fixed time during electrophoresis.
For a given potential difference, state two other factors that will affect how far a given
amino acid travels in a fixed time during electrophoresis.
1. .......................................................................................................................................
1. .......................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
2. .......................................................................................................................................
14

2. .......................................................................................................................................
14 B
Section
...........................................................................................................................................
[2]
Section in B
...........................................................................................................................................
Answer all the questions the spaces provided.
(c) A number of analytical [2]
Answerand all theseparation
questionstechniques
in the spaces rely on substances having different
provided.
partition coefficients.
9 (a) A
86 (c) A number
mixture of of amino
analytical acids andcanseparation
be separated by electrophoresis.
techniques rely on substancesDuring anhaving electrophoresis
different
experiment,
partition coeffi cients.
9
6 (a) AState whatofisamino
mixture meantacids by the cantermbe partition
separated coeffi cient.
by electrophoresis. During an electrophoresis
experiment,
● different amino acids move in different directions,
State what is meant by the term partition coefficient.
...........................................................................................................................................
● different amino acids move at different speeds,
●● different
some aminoamino acids
acids domove in different
not move at all. directions,
...........................................................................................................................................
● different amino acids move at different speeds,
...........................................................................................................................................
●Explain
some amino
these acids do not move at all.
observations.
...........................................................................................................................................
...........................................................................................................................................
Explain these observations.
....................................................................................................................................................
[1]
...........................................................................................................................................
....................................................................................................................................................
....................................................................................................................................................
[1]
....................................................................................................................................................
....................................................................................................................................................

....................................................................................................................................................
.............................................................................................................................................. [3]

.............................................................................................................................................. [3]
(b)2013
© UCLES (i) A mixture of amino acids can also be separated by thin-layer chromatography.
9701/41/O/N/13
Identify the mobile and the stationary phases in this type of chromatography.
(b)2013
© UCLES (i) A mixture of amino acids can also be separated by thin-layer chromatography.
9701/41/O/N/13
Identify the mobile and the stationary phases in this type of chromatography.
mobile phase ......................................................................................................................

mobile phase
stationary ......................................................................................................................
phase .................................................................................................................

(ii) stationary
What is thephase .................................................................................................................
process by which thin-layer chromatography can separate a mixture?

(ii) What is the process by which thin-layer chromatography can separate a mixture?
.............................................................................................................................................
[3]
.............................................................................................................................................
(c) State three structural features of DNA. [3]

(c) State three structural features of DNA.

....................................................................................................................................................

....................................................................................................................................................
....................................................................................................................................................

....................................................................................................................................................
.............................................................................................................................................. [3]

..............................................................................................................................................
CEDAR COLLEGE ELECTROPHORESIS WS [3] 1
Electrophoresis
CEDAR COLLEGE 2 Bilal Hameed
ELECTROPHORESIS WS 1