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Circular dichroism and UV resonance raman study of the impact of alcohols on the gibbs free energy landscape of an α-helical peptide

Xiong, K and Asher, SA (2010) Circular dichroism and UV resonance raman study of the impact of alcohols on the gibbs free energy landscape of an α-helical peptide. Biochemistry, 49 (15). 3336 - 3342. ISSN 0006-2960

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Abstract

We used CD and UV resonance Raman spectroscopy to study the impact of alcohols on the conformational equilibria and relative Gibbs free energy landscapes along the Ramachandran φ-coordinate of a mainly poly-Ala peptide, AP with an AAAAA(AAARA)3A sequence. 2,2,2-Trifluoroethanol (TFE) most stabilizes the α-helix-like conformations, followed by ethanol, methanol, and pure water. The π-bulge conformation is stabilized more than the α-helix, while the 310-helix is destabilized due to the alcohol-increased hydrophobicity. Turns are also stabilized by alcohols. We also found that while TFE induces more α-helices, it favors multiple, shorter helix segments. © 2010 American Chemical Society.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Xiong, K
Asher, SAasher@pitt.eduASHER
Date: 20 April 2010
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 49
Number: 15
Page Range: 3336 - 3342
DOI or Unique Handle: 10.1021/bi100176a
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: Alcohols--pharmacology; Amino Acid Sequence; Circular Dichroism; Ethanol--pharmacology; Indicators and Reagents; Methanol--pharmacology; Models, Molecular; Peptides--chemistry; Peptides--drug effects; Protein Conformation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Thermodynamics; Water--chemistry
Other ID: NLM NIHMS188980, NLM PMC2857330
PubMed Central ID: PMC2857330
PubMed ID: 20225890
Date Deposited: 08 Feb 2013 20:56
Last Modified: 22 Jun 2021 13:55
URI: http://d-scholarship.pitt.edu/id/eprint/17246

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