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Circular dichroism and ultraviolet resonance raman indicate little Arg-Glu side chain α-helix peptide stabilization

Hong, Z and Ahmed, Z and Asher, SA (2011) Circular dichroism and ultraviolet resonance raman indicate little Arg-Glu side chain α-helix peptide stabilization. Journal of Physical Chemistry B, 115 (14). 4234 - 4243. ISSN 1520-6106

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Electrostatic interactions between side chains can control the conformation and folding of peptides and proteins. We used circular dichroism (CD) and ultraviolet (UV) resonance Raman spectroscopy (UVRR) to examine the impact of side chain charge on the conformations of two 21 residue mainly polyala peptides with a few Arg and Glu residues. We expected that attractions between Arg-10 and Glu-14 side chains would stabilize the α-helix conformation compared to a peptide with an Arg-14. Surprisingly, CD suggests that the peptide with the Glu-14 is less helical. In contrast, the UVRR show that these two peptides have similar α-helix content. We conclude that the peptide with Glu-14 has the same net α-helix content as the peptide with the Arg but has two α-helices of shorter length. Thus, side chain interactions between Arg-10 and Glu-14 have a minor impact on α-helix stability. The thermal melting of these two peptides is similar. However the Glu-14 peptide pH induced melting forms type III turn structures that form α-helix-turn-α-helix conformations. © 2011 American Chemical Society.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Hong, Z
Ahmed, Z
Asher, SAasher@pitt.eduASHER
Date: 14 April 2011
Date Type: Publication
Journal or Publication Title: Journal of Physical Chemistry B
Volume: 115
Number: 14
Page Range: 4234 - 4243
DOI or Unique Handle: 10.1021/jp112238q
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1520-6106
MeSH Headings: Circular Dichroism; Dipeptides--chemistry; Hydrogen-Ion Concentration; Peptides--chemistry; Protein Structure, Secondary; Spectrum Analysis, Raman; Static Electricity; Temperature; Thermodynamics; Ultraviolet Rays
Other ID: NLM NIHMS283040, NLM PMC3074482
PubMed Central ID: PMC3074482
PubMed ID: 21425805
Date Deposited: 08 Feb 2013 20:55
Last Modified: 02 Feb 2019 16:55


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