eprintid: 17215
rev_number: 26
userid: 1419
dir: disk0/00/01/72/15
datestamp: 2013-02-08 21:11:48
lastmod: 2021-06-12 23:55:33
status_changed: 2013-02-08 21:11:48
type: article
metadata_visibility: show
item_issues_count: 0
eprint_status: archive
creators_name: Ahmed, Z
creators_name: Asher, SA
creators_email:
creators_email: asher@pitt.edu
creators_id:
creators_id: ASHER
title: UV resonance Raman investigation of a 310-helical peptide reveals a rough energy landscape
ispublished: pub
divisions: sch_as_chemistry
full_text_status: public
abstract: We used UVRRS at 194 and 204 nm excitation to examine the backbone conformation of a 13-residue polypeptide (gp41659-671) that has been shown by NMR to predominantly fold into a 310-helix. Examination of the conformation sensitive AmIII3 region indicates the peptide has significant populations of β-turn, PPII, 310-helix, and π-helix-like conformations but little α-helix. We estimate that at 1 °C on average six of the 12 peptide bonds are in folded conformations (predominantly 310- and π-helix), while the other six are in unfolded (β-turn/PPII) conformations. The folded and unfolded populations do not change significantly as the temperature is increased from 1 to 60 °C, suggesting a unique energy landscape where the folded and unfolded conformations are essentially degenerate in energy and exhibit identical temperature dependences. © 2006 American Chemical Society.
date: 2006-08-01
date_type: published
publication: Biochemistry
volume: 45
number: 30
pagerange: 9068 - 9073
refereed: TRUE
issn: 0006-2960
id_number: 10.1021/bi060858m
pmid: 16866352
mesh_headings: HIV Envelope Protein gp41--chemistry
mesh_headings: Peptide Fragments--chemistry
mesh_headings: Protein Conformation
mesh_headings: Protein Structure, Secondary
mesh_headings: Spectrophotometry, Ultraviolet--methods
mesh_headings: Spectrum Analysis, Raman--methods
mesh_headings: Temperature
mesh_headings: Thermodynamics
chemical_names: HIV Envelope Protein gp41
chemical_names: Peptide Fragments
citation: Ahmed, Z and Asher, SA (2006) UV resonance Raman investigation of a 310-helical peptide reveals a rough energy landscape. Biochemistry, 45 (30). 9068 - 9073. ISSN 0006-2960
document_url: http://d-scholarship-dev.library.pitt.edu/17215/1/licence.txt