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Biology

Protein(Fundamental)
(a) classify amino acids into four main classes based on their side chains: polar, non-polar, acidic and basic;
(b) describe the structure of an amino acid and the formation of peptide bonds in polypeptides;
(c) explain the properties of protein (amphoteric, isoelectric point, buffer and colloid);
(d) differentiate the various levels of organisation of protein structure (primary, secondary, tertiary and quaternary)
and relate the functions of each structure to the organisation of proteins;
(e) explain the denaturation and renaturation of protein;
(f) classify proteins according to their structures, compositions (simple and conjugated) and functions.

1. Consist of______,________,_______,_______,________,
sometimes a little bit ________, __________.
2. Monomer: __________
3. DRAW the structure of amino acid:

4. 20 types of different amino acids have different R groups.


5. R groups give the a.a theirs own _________. The
___________________is based on its _________.

(a) classify amino acids into four main classes based on their side chains: polar, non-polar, acidic and basic;
6. A.A are __________, -each a.a consists of_______&________

7. BASIC / Acidic a.a


Produce ________(-basic), ________(-acidic) charged ion &
strongly ___________
8. Proteins derived from these a a, (e.g. globular protein are ______in
water.
9. 3-dimensional structure of a globular protein is stabilised by the
______________________________________in the molecule

10. A. a. with non-polar hydrocarbons side chains


 - Protein that consist of a large amount of such a, a, are
_________ & _______________
 - Usually form a __________ protein, e.g. __________
 The side chain is _______ & the a.a are ______________
11. A.a with polar R groups produce ________________ but do
not _________ or ___________ electrons
 Increase ___________________ & enables__________________
 The R groups of these a.a are more _________ in water
(more________) than those of the nonpolar a.a, because they
contain functional groups that _________________ with h2o

STPM 2020
1. AMINO ACID ARE CLASSIFIED INTO 4 MAIN GROUPS BASED ON
PROPERTIES OF THEIR SIDE CHAIN. DIFFERENTIATE BWT POLAR
AND NON-POLAR AMINO ACID GROUPS (5m)

 Polar a.a side chains contains groups that are____________ while non-polar
amino acid side chains are ___________
(R-group determine the characteristics of amino acid)
 Polar amino acid side chains ______ form _______________whereas non-
polar amino acid side chains ______ form _______________
 Polar amino acid are __________in nature while non-polar amino acids are
____________ in nature
 Polar a.a are found in the ___________ of the protein structure and can
_______ water while non polar a.a are found in the _______ of the protein
structure and ______ from water
2. TRIAL PAPER SMJK PEREMPUAN CINA PENANG 2022 (q18)
The variation in the side chains (R groups) of amino acids is important in both intramolecularand intermolecular interactions in a
protein.

Describe how different side chains (R groups) of amino acid groups the amino acids and determines the structure and functions of
the protein. Give an example of amino acid for each group. (15)
0
(b) describe the structure of an amino acid and the formation of peptide bonds in polypeptides;

1. The amino acid group and the carboxyl group of a pair of amino
acids can undergo ___________ reaction to form covalent bond call
_____________.
2. Dimmer: ______________
3. Draw the structure of dimmer:

4. How to differentiate type of protein?


 __________________________________________________
 __________________________________________________
 __________________________________________________

5. Protein molecules can also conjugates with other


_________________ to form a new structure

(d) differentiate the various levels of organisation of protein structure (primary, secondary, tertiary and quaternary)

1. Primary structure
 Organisation: ___________________________
 Sequences determine by ________________
 The sequence of a.a determines the ____________ of the
protein formed in other level

2. Secondary Structure
o The ____________ and ___________ o

alpha helix (α-helix)
Shape: _____________ maintain by ________ bond
Example:

 _________ (protein in hair and nail, is in the form of a ______


helix)
 _________ (protein in tendons, ligaments and cartilage has a
_______ helical shape)

 beta sheet, (β-sheet) (also β-pleated sheet)

Shape: polypeptide chains are arranged ________ &_________ to each other

Held together by_________ but folded ____________

Has a high resistance to _________, ____________ but flexible

Example: ___________
3. Tertiary Structure
o What is tertiary structure of protein
Single _________________ are ______& ________ to form 3D shape
__________
Held by what bond?
o _______________
o _______________
o _______________
o _______________
o _______________
Example of tertiary structure:

o ____________________
o ____________________
4. Quaternary Structure
o ________________________ polypeptide chains bound and associated together into one functional
molecule.
Held by what bond?
o _______________
o _______________
o _______________
o _______________
o _______________
o Example: ______________________________________________________________________

STPM 2011
DESCRIBE THE INTERACTION WHICH CONTRIBUTE TO THE TERTIARY
STRUCTURE OF PROTEIN.

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