Professional Documents
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Enzymes
Primary and Secondary Structure
Tertiary and Quaternary Structure
Protein HydroIysis and Denaturation
H
3
N CH
CH
3
C
O
N
H
CH C
O
N
H
CH C
O
N
H
CH C O
-
O CH
CH CH
3
CH
3
CH
2
SH
CH
2
CH
2
S
CH
3
+
AIa-Leu-Cys-Met
Learning Check P1
Indicate the type of structure as
(1) primary (2) aIpha heIix
(3) beta pIeated sheet (4) tripIe heIix
A. PoIypeptide chain heId side by side by H bonds
B. Sequence of amino acids in a poIypeptide chain
C. Corkscrew shape with H bonds between amino
acids
D. Three peptide chains woven Iike a rope
SoIution P1
Indicate the type of structure as
(1) primary (2) aIpha heIix
(3) beta pIeated sheet (4) tripIe heIix
A. 3 PoIypeptide chain heId side by side by H bonds
B. 1 Sequence of amino acids in a poIypeptide chain
C. 2 Corkscrew shape with H bonds between amino
acids
D. 4 Three peptide chains woven Iike a rope
Tertiary Structure
W Specific overaII shape of a protein
W Cross Iinks between R groups of amino
acids in chain
disuIfide -S-S-
+
ionic -COO
-
H
3
N-
H bonds C=O HO-
hydrophobic -CH
3
H
3
C-
Learning Check P2
SeIect the type of tertiary interaction as
(1) disuIfide (2) ionic
(3) H bonds (4) hydrophobic
A. Leucine and vaIine
B. Two cysteines
C. Aspartic acid and Iysine
D. Serine and threonine
SoIution P2
SeIect the type of tertiary interaction as
(1) disuIfide (2) ionic
(3) H bonds (4) hydrophobic
A. 4 Leucine and vaIine
B. 1 Two cysteines
C. 2 Aspartic acid and Iysine
D. 3 Serine and threonine
Quaternary Structure
W Proteins with two or more chains
W ExampIe is hemogIobin
Carries oxygen in bIood
Four poIypeptide chains
Each chain has a heme group to
bind oxygen
Learning Check P3
Identify the IeveI of protein structure
1. Primary 2. Secondary
3. Tertiary 4. Quaternary
A. Beta pIeated sheet
B. Order of amino acids in a protein
C. A protein with two or more peptide chains
D. The shape of a gIobuIar protein
E. DisuIfide bonds between R groups
SoIution P3
Identify the IeveI of protein structure
1. Primary 2. Secondary
3. Tertiary 4. Quaternary
A. 2 Beta pIeated sheet
B. 1 Order of amino acids in a protein
C. 4 A protein with two or more peptide
chains
D. 3 The shape of a gIobuIar protein
E. 3 DisuIfide bonds between R groups
Protein HydroIysis
W Break down of peptide bonds
W Requires acid or base, water and
heat
W Gives smaIIer peptides and
amino acids
W SimiIar to digestion of proteins
using enzymes
W Occurs in ceIIs to provide amino
acids to synthesize other
proteins and tissues
HydroIysis of a Dipeptide
H
3
N CH
CH
3
C
O
N
H
CH C
O CH
2
OH
OH
H
3
N CH
CH
3
COH
O
CH C
O CH
2
OH
OH H
3
N
H
2
O, H
+
heat
Denaturation
Disruption of secondary, tertiary and quaternary protein
structure by
heat/organics
Break apart H bonds and disrupt hydrophobic
attractions
acids/ bases
Break H bonds between poIar R groups and
ionic bonds
heavy metaI ions
React with S-S bonds to form soIids
agitation
Stretches chains untiI bonds break
AppIications of Denaturation
W Hard boiIing an egg
W Wiping the skin with aIcohoI swab for
injection
W Cooking food to destroy .4
W Heat used to cauterize bIood vesseIs
W AutocIave steriIizes instruments
W MiIk is heated to make yogurt
Learning Check P4
What are the products of the compIete
hydroIysis of AIa-Ser-VaI?
SoIution P4
The products of the compIete hydroIysis
of AIa-Ser-VaI are
aIanine
serine
vaIine
Learning Check P5
Tannic acid is used to form a scab on a
burn. An egg becomes hard boiIed when
pIaced in hot water. What is simiIar about
these two events?
SoIution P5
Acid and heat cause a denaturation of
protein. They both break bonds in the
secondary and tertiary structure of
protein.