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Computational and experimental determination of the α-helix unfolding reaction coordinate

Asciutto, EK and Mikhonin, AV and Asher, SA and Madura, JD (2008) Computational and experimental determination of the α-helix unfolding reaction coordinate. Biochemistry, 47 (7). 2046 - 2050. ISSN 0006-2960

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We demonstrate a calculated α-helix peptide folding energy landscape which accurately simulates the first experimentally measured α-helix melting energy landscape. We examine a 21-amino acid, mainly polyalanine peptide and calculate the free energy along the Ψ Ramachandran angle secondary folding coordinate. The experimental free energy landscape was determined using UV resonance Raman spectroscopy. The relative free energy values are very close as are the equilibrium peptide conformations. We find 2.3 kcal/mol activation barriers between the α-helix-like and PPII-like basins. We also find that the α-helix-like conformations are quite defective and the α-helix-like structure dynamically samples 310-helix and π-bulges. © 2008 American Chemical Society.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Asciutto, EK
Mikhonin, AV
Asher, SAasher@pitt.eduASHER
Madura, JD
Date: 19 February 2008
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 47
Number: 7
Page Range: 2046 - 2050
DOI or Unique Handle: 10.1021/bi702112v
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: Protein Denaturation; Spectrum Analysis, Raman
PubMed ID: 18189423
Date Deposited: 08 Feb 2013 21:06
Last Modified: 22 Jun 2021 13:55


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