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Q1: Answer Two of The Following Questions: (50 Points)

This document contains questions for a postgraduate chemistry exam focusing on protein engineering. It asks students to answer two of three multi-part questions. Question 1 involves calculating properties of the muscle protein tropomyosin based on its molecular weight and composition, identifying products of various enzymatic digestions of a peptide sequence, and explaining site-directed mutagenesis. Question 2 involves answering a question in a Google form. Question 3 gives a choice between parts A and B, with part A asking about protein renaturation, differences between peptide sequences, inducing curls in hair, random coil regions, and differences between alpha-helices and beta-sheets. Part B asks about methods of breaking S-S bonds in proteins, limitations on peptide
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0% found this document useful (0 votes)
45 views2 pages

Q1: Answer Two of The Following Questions: (50 Points)

This document contains questions for a postgraduate chemistry exam focusing on protein engineering. It asks students to answer two of three multi-part questions. Question 1 involves calculating properties of the muscle protein tropomyosin based on its molecular weight and composition, identifying products of various enzymatic digestions of a peptide sequence, and explaining site-directed mutagenesis. Question 2 involves answering a question in a Google form. Question 3 gives a choice between parts A and B, with part A asking about protein renaturation, differences between peptide sequences, inducing curls in hair, random coil regions, and differences between alpha-helices and beta-sheets. Part B asks about methods of breaking S-S bonds in proteins, limitations on peptide
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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University of Baghdad Postgraduate Studies (PhD)

College of Science Semester: Second


Department of Biotechnology Subject: Chemistry and
Date: 18/ 6/ 2020 protein engineering

Q1: Answer two of the Following questions: (50 points)


A: The tropomyosin (muscle protein) consists of two identical chains and the molecular weight of this
protein is 70 kDa. Can you calculate the length of α-helix and open chain of protein. (The average of
MW of amino acid 110 Da.)

B: 1- Determine the products resulting from the following treatment of peptide sequences.
- Trypsin digestion
- Chymotrypsin digestion
- Carboxy peptidase
- FDNB
- CNBr

Ala-Glu-Lys-Phe-Met-Cys-Tyr-Met-Gly-phe

2- In what order would the amino acids Arg, His and Leu be eluted from DEAE-cellulose
column at pH 8.1? In what order would Glu, Lys and Val be eluted for CMC column at pH 6.2
(PI of amino acid are: Arg: 10.76, His: 7.64, Leu: 6.04, Glu: 3.08, Lys: 9.74, Val: 6.02)

C: Explain (by drawing only) the alteration of amino acid sequence by site-directed mutagenesis?
What are the advantages of protein modification?

Q2: Answer the question in the Google form file. : (20 points)

Q3) Answer either A or B of the following questions : ( 30 points )

A: Answer each of the following?


1- Give enough time, can all denatured proteins spontaneously renature? Why?
2- Why are the tetra peptides (Ala- Gly- Ser- Ala) and (Ala- Ser- Gly- Ala) not identical?
3- The shape of hair is determined by the pattern of disulfide bond in keratin (it is major protein).
How can curls be induced?
4- List the cases which cause the random coil regions in protein structure?
5- What are the differences between alpha-helix and Beta-sheet protein conformation?
B: Answer each of the following? (30 degree)
1) What are the chemical hydrolysis methods of S-S bond in protein sequence?

2) The conformational freedom of peptide bonds is limited, why?

3) Under physiological condition, poly lysin assumes a random coil conformation. Under what
condition it might form α-helix?

4) Which peptide has great absorbance at 280 nm.


a- Gln- Leu- Glu- Phe- Thr- Leu- Asp- Gly- Tyr.
b- Ser- Val- Trp- Asp- Phe- Gly- Tyr- Trp- Ala.

5) Write all the quaternary forms possible for a hexmeric protein composed β and α type subunits.
(Homo hexamers are allowed). What forces likely bind the subunits to each other.

Good luck
Dr. Ghazi M. Aziz

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