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Tutorial 2_Questions_Student version 2

The document is a tutorial for a General Biochemistry course at Hong Kong Community College, focusing on protein properties and structures. It includes keywords, matching questions, classification of amino acids, and multiple-choice questions related to protein structure and function. Key concepts covered include primary, secondary, tertiary, and quaternary structures, as well as specific amino acid classifications and their roles in protein functionality.

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Him Ng
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2 views5 pages

Tutorial 2_Questions_Student version 2

The document is a tutorial for a General Biochemistry course at Hong Kong Community College, focusing on protein properties and structures. It includes keywords, matching questions, classification of amino acids, and multiple-choice questions related to protein structure and function. Key concepts covered include primary, secondary, tertiary, and quaternary structures, as well as specific amino acid classifications and their roles in protein functionality.

Uploaded by

Him Ng
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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Hong Kong Community College

SEHH2231 General Biochemistry

Tutorial 2: Protein Properties I

KEYWORDS TO STUDY :
Linear sequence of amino acids Ionic bonds Collagen
Peptide Disulfide bonds/bridges Collagen fibrils
Peptide bond Hydrophobic interactions Tropocollagen
Polypeptide Fibrous protein Myoglobin
-helix (singular) [-helices (plural)] Globular protein Haemoglobin or Hemoglobin
-sheet [-sheets] Membrane protein Monomeric or monomer
-turn or -bend [-turns or -bends] -keratin Dimeric or dimer
Motif (Supersecondary structure) Protofilament Haemolysis or hemolysis
Subunit/domain Protofibril Anaemia or anemia
Hydrogen bonds Silk fibroin Insulin receptor

Question 1: Match each term (in the left-hand column) with its description (in the right-hand column):
(a) Primary structure 1. Forms between two cysteine residues
(b) Peptide bond 2. Basic component of quaternary structure
(c) Disulfide bond 3. A rodlike structure with a tightly coiled or spiral backbone
(d) -helix 4. Refers to the arrangements of the subunits and the nature

(e) -sheet or -pleated sheet of their interactions

(f) Secondary structure 5. Formed by hydrogen bonds between parallel or

(g) Tertiary structure antiparallel chains


6. Refers to the spatial arrangement of amino acid residues
(h) Supersecondary structure
that are far apart in the sequence.
(i) Subunit
7. Folding of linear amino acid sequences
(j) Quaternary structure
8. The bond responsible for primary structure
9. Combinations of secondary structure are present in many
proteins
10. Sequence of amino acids in a protein
Question 2: Classify each amino acid (in the right-hand column) into its corresponding class based on the side
chain types (in the left-hand column):

(a) Non-polar side chain 1. Glutamine 12. Proline


(b) Uncharged polar side chain 2. Glycine 13. Cysteine
(c) Acid side chain 3. Histidine 14. Serine
(d) Basic side chain 4. Leucine 15. Alanine
(e) Aromatic side chain 5. Tryptophan 16. Aspartic acid
6.Asparagine 17. Methionine
7. Threonine 18. Phenylalaine
8. Valine 19. Serine
9. Arginine 20. Isoleucine
10. Tyrosine 21. Lysine
11. Glutamatic acid

Question 3: Match each amino acid (in the left-hand column) with the appropriate side-chain type (in the right-
hand column):
(a) Leu 1. Acidic side chain
(b) Glu 2. Basic side chain
(c) Lys 3. Sulfur-containing (or sulphur-containing) side chain
(d) Cys 4. Aromatic side chain
(e) Trp 5. Non-polar side chain

Question 4:
What are the levels of protein structure? Describe the types of bonds characteristic of each level.

Question 5:
The shape of hair is determined in part of the pattern of disulfide bonds in -keratin which is its major protein.
How can curls be induced?
Question 2: Classify each amino acid (in the right-hand column) into its corresponding class based on the side
chain types (in the left-hand column):

(a) Non-polar side chain 1. Glutamine 12. Proline


(b) Uncharged polar side chain 2. Glycine 13. Cysteine
(c) Acid side chain 3. Histidine 14. Serine
(d) Basic side chain 4. Leucine 15. Alanine
(e) Aromatic side chain 5. Tryptophan 16. Aspartic acid
6.Asparagine 17. Methionine
7. Threonine 18. Phenylalaine
8. Valine 19. Serine
9. Arginine 20. Isoleucine
10. Tyrosine 21. Lysine
11. Glutamatic acid

Question 3: Match each amino acid (in the left-hand column) with the appropriate side-chain type (in the right-
hand column):
(a) Leu 1. Acidic side chain
(b) Glu 2. Basic side chain
(c) Lys 3. Sulfur-containing (or sulphur-containing) side chain
(d) Cys 4. Aromatic side chain
(e) Trp 5. Non-polar side chain

Question 4:
What are the levels of protein structure? Describe the types of bonds characteristic of each level.

Question 5:
The shape of hair is determined in part of the pattern of disulfide bonds in -keratin which is its major protein.
How can curls be induced?
Question 6:
Predict which regular, repeating structure is more likely for two polypeptides
(a) poly(Gly-Ala-Gly-Thr)
(b) poly(Glu-Ala-Leu-His)
Given the following information is provided:
Helix formers Glu, Ala, Leu, His, Met, Gln, Trp, Val, Phe, Lys, Ile
Helix breakers Pro, Gly, Tyr, Asn
Indifferent residues to helix Asp, Thr, Ser, Arg, Cys
-sheet former Ala, Gly
-sheet breaker Bulky side chain, e.g. His, Trp, Tyr, Phe

Multiple choice questions:


1. An amino acid that is incompatible with a -helix is
A. Tyrosine
B. Tryptophan
C. Valine
D. Proline
E. Asparagine

2. Collagen is unique in that it contains much ______________ and _______________.


(i) Proline
(ii) Lysine
(iii) Hydroxyproline
(iv) hydroxylysine

A. (i) and (ii) only


B. (i) and (iii) only
C. (ii) and (iii) only
D. (ii) and (iv) only
E. (iii) and (iv) only

3. An important structural features of antibodies is that


A. they are composed of two peptide chains.
B. they are composed of a single peptide chain.
C. they are composed of two long and two short peptide chains.
D. they cannot be dissociated by chemical degradation.
E. they do not contain sulfur-containing (or sulphur-containing) amino acids.
4. The ability of proteins to absorb ultraviolet light is a property of the amino acids with:
A. nonpolar side chain.
B. uncharged polar side chain.
C. acidic side chain.
D. basic side chain.
E. Aromatic side chain.

5. Proline is distinct among the 21 commonly found amino acids because


A. it is a 6-membered ring compound.
B. it is hydrophilic and ionic.
C. the nitrogen of the amino group is in a ring.
D. the carbon of the carboxyl group is in a ring.
E. It has no effect on protein structure.

6. The ability of haemoglobin to serve as an effective transporter of oxygen and carbon dioxide between lungs
and tissues is explained by which of the following properties?
A. The isolated heme group with ferrous iron binds oxygen much more avidly than carbon dioxide.
B. The - and -globin chains of haemoglobin have very different primary structures than myoglobin
C. Haemoglobin utilizes oxidized ferric iron to bind oxygen, in contrast to the ferrous iron of myoglobin
D. In contrast to myoglobin, haemoglobin exhibits greater changes in secondary and tertiary structure
after oxygen binding.
E. Haemoglobin binds proportionately more oxygen at low oxygen tension than does myoglobin.

7. The substitution of valine for glutamate at position 6 on the two -chains in sickle cell haemoglobin causes
which of the following?
A. Decreased polymerization of deoxyhaemoglobin
B. Increased electrophoretic mobility at pH 7
C. Increased solubility of deoxyhaemoglobin
D. More flexible red blood cells
E. Unchanged primary structure

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