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Which peptide has greater absorbance at 280 nm?

A. Gln–Leu–Glu–Phe–Thr–Leu–Asp–Gly–Tyr

B. Ser–Val–Trp–Asp–Phe–Gly–Tyr–Trp–Ala

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–Leu–Glu–Phe–Thr–Leu–Asp–Gly–Tyr sequence. In this amino acid sequence, there is absence of tryptophan amino acids which has the highest absorbance. However, peptide B has Ser–Val–Trp–Asp–Phe–Gly–Tyr–Trp–Ala 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

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?

You are using ammonium sulphate to purify protein Q (pI = 5.0) by salting out from a solution at pH 7.0. How should you adjust the pH of the mixture to maximize the amount of protein Q that precipitates?

(a) The ESI-MS spectrum below was obtained for hen egg-white lysozyme (HEWL). Using peaks 5 and 6, calculate the molecular mass of HEWL (see Sample Calculation 5-1).

[http://www.astbury.leeds.ac.uk/facil/MStut/mstutorial.htm. Published by A.E. Ashcroft, Astbury Centre for Structural Molecular Biology, University of Leeds (2000)]

(b) What is the charge on the ion that makes peak 5?

Explain the origin of orthologous proteins, paralogous proteins, and multidomain proteins.

Consult Table 5-1 to complete the following: (a) On a plot of absorbance at 280 nm versus elution volume, sketch the results of gel filtration of a mixture containing human cytochrome c and bacteriophage T7 RNA polymerase and identify each peak. (b) Sketch the results of SDS-PAGE of the same protein mixture showing the direction of migration and identifying each band.

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