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Chapter 5: Q5-3P (page 127)

Which peptide has greater absorbance at 280 nm?

A. Gln鈥揕eu鈥揋lu鈥揚he鈥揟hr鈥揕eu鈥揂sp鈥揋ly鈥揟yr

B. Ser鈥揤al鈥揟rp鈥揂sp鈥揚he鈥揋ly鈥揟yr鈥揟rp鈥揂la

Short Answer

Expert verified

Peptide B has greater absorbance because it has tryptophan and other aromatic residues.

Step by step solution

01

Tryptophan has greatest absorbance

Tryptophan has the greatest absorbance at 280nm because of its higher resonance energy transfer. Also, the fluorescence spectrum of aromatic residues such as tyrosine and phenylalanine resembles that of tryptophan.

02

Peptide B had greater absorbance

Peptide A has Gln鈥揕eu鈥揋lu鈥揚he鈥揟hr鈥揕eu鈥揂sp鈥揋ly鈥揟yr sequence. In this amino acid sequence, there is absence of tryptophan amino acids which has the highest absorbance. However, peptide B has Ser鈥揤al鈥揟rp鈥揂sp鈥揚he鈥揋ly鈥揟yr鈥揟rp鈥揂la sequence. In this amino acid sequence, there is presence of tryptophan amino acids which has the highest absorbance due to its greater absorptivity.

Hence, peptide B has greater absorbance.

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Most popular questions from this chapter

What fractionation procedure could be used to purify protein 1 from a mixture of three proteins whose amino acid compositions are as follows?

1. 25% Ala, 20% Gly, 20% Ser, 10% Ile, 10% Val, 5% Asn, 5% Gln, 5% Pro

2. 30% Gln, 25% Glu, 20% Lys, 15% Ser, 10% Cys

3. 25% Asn, 20% Gly, 20% Asp, 20% Ser, 10% Lys, 5% Tyr

All three proteins are similar in size and pI, and there is no antibody available for protein 1.

You must cleave the following peptide into smaller fragments. Which of the proteases listed in Table 5-4 would be likely to yield the most fragments? The fewest?

NMTQGRCKPVNTFVHEPLVDVQNVCFKE

You wish to determine the sequence of a polypeptide that has the following amino acid composition.

1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1 Gln 4 Glu 1 His 1 Lys 1 Met 1 Phe 2 Pro 4 Ser 2 Tyr 1 Trp

(a) What is the maximum number of peptides you can expect if you cleave the polypeptide with cyanogen bromide?

(b) What is the maximum number of peptides you can expect if you cleave the polypeptide with chymotrypsin?

(c) Analysis of the intact polypeptide reveals that there are no free sulfhydryl groups. How many disulfide bonds are likely to be present?

(d) How many different arrangements of disulfide bonds are possible?

Electrospray ionization mass spectrometry (ESI-MS) of proteins involves creating positively charged ions of the protein and separating them according to their mass-to-charge ratio (m/z).

(a) What causes the different positive charges on different particles of the protein?

(b) The amino acid composition (in numbers of residues per chain) of hen egg-white lysozyme (HEWL) is as follows:

P 2 Y 3 N 14 H 1

D 7 M 2 L 8 E 2

C 8 R 11 G 12 F 3

A 12 I 6 K 6 V 6

S 10 W 6 T 7 Q 3

What is the maximum positive charge that can be present on a HEWL ion?

Question: Sketch a phylogenetic tree for the family of homologous proteins

whose partial sequences are given below.

Protein A T L A D K A I S L H D S

Protein B T L G D K A V S I H E S

Protein C T L A D K A I S V H D S
See all solutions

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