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1. You wish to determine the sequence of a polypeptide that hashe following amino acid compostion:

1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1Gln 4 Glu

1 His 1 Lys 1 Met 1Phe 2 Pro 4 Ser 2Tyr 1Trp

A- What is the maximum number of peptides you can expect if youcleave the polypeptide with cyanogen bromide?

B- What is the maximum number of peptides you can expect if youcleave the polypeptide with chemotropism?

C- Analysis of the intact polypeptide reveals that there are nofree sulfhydryl groups. How many different disulfide bonds arelikely to be present?

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Beverley Smith
Beverley SmithLv2
28 Sep 2019
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Related questions

Please help me with this question,

1. At pH 7.0, in what order would the following three peptides be eluted from a column filled with an anion-exchange polymer? Their amino acid compositions are:

Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.

Peptide B: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%.

Peptide C: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.

First off column: _______________ Second: _______________ Last off column: _______________

Answer the following questions concerning the polypeptides whose amino acid sequences are shown below. Explain your reasoning for all.

A) Gly-Ile-Trp-Leu-Ile-Ile-Phe-Gly-Val-Val-Ala-Gly-Val-Ile-Gly-Trp-Ile-Leu-Leu-Leu

B) Gly-Pro-Asp-Gly-Pro-Met-Gly-Pro-Ser-Gly-Pro-Arg-Gly-Pro-Glu-Gly-Pro-Asp-Gly

C) Gly-Met-Trp-Pro-Glu-Met-Cys-Gly-Glu-Pro-Ala-His-Val-Arg-Asp-Tyr-Pro-Leu-Leu

D) Gly-Met-Trp-Pro-Glu-Met-Cys-Gly-Glu-Pro-Ala-His-Val-Arg-Asp-Tyr-Cys-Leu-Leu

1. Which would be most likely to form an a-helical structure?

2. Which could have at least one disulfide bond?

3. Suppose that the first amino acid residue in peptide (1) were altered from Gly to Pro. Would you expect this change to have an effect on the secondary structure of this peptide? Why or why not?

4. It is possible to make some predictions about protein secondary structure based on the primary sequence. Consider the following amino acid sequence.

Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg

(a) Where might B turns occur?

(b) Where might intrachain disulfide cross-linkages be formed?

(c) Assuming that this sequence is part of a larger globular protein, what is the probable location (exterior or interior of the protein) of the amino acid residues and explain your reasoning.

Asp Ile Thr Ala Gln Lys

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