eprintid: 17225
rev_number: 22
userid: 1419
dir: disk0/00/01/72/25
datestamp: 2013-02-08 21:06:00
lastmod: 2021-06-12 23:55:35
status_changed: 2013-02-08 21:06:00
type: article
metadata_visibility: show
item_issues_count: 0
eprint_status: archive
creators_name: Asciutto, EK
creators_name: Mikhonin, AV
creators_name: Asher, SA
creators_name: Madura, JD
creators_email: 
creators_email: 
creators_email: asher@pitt.edu
creators_email: 
creators_id: 
creators_id: 
creators_id: ASHER
creators_id: 
title: Computational and experimental determination of the α-helix unfolding reaction coordinate
ispublished: pub
divisions: sch_as_chemistry
full_text_status: public
abstract: 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.
date: 2008-02-19
date_type: published
publication: Biochemistry
volume: 47
number: 7
pagerange: 2046 - 2050
refereed: TRUE
issn: 0006-2960
id_number: 10.1021/bi702112v
pmid: 18189423
mesh_headings: Protein Denaturation
mesh_headings: Spectrum Analysis, Raman
citation:   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     
document_url: http://d-scholarship-dev.library.pitt.edu/17225/1/licence.txt