relation: http://d-scholarship-dev.library.pitt.edu/17215/
title: UV resonance Raman investigation of a 3<inf>10</inf>-helical peptide reveals a rough energy landscape
creator: Ahmed, Z
creator: Asher, SA
description: 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
type: Article
type: PeerReviewed
format: text/plain
language: en
rights: attached
identifier: http://d-scholarship-dev.library.pitt.edu/17215/1/licence.txt
identifier:   Ahmed, Z and Asher, SA  (2006) UV resonance Raman investigation of a 3<inf>10</inf>-helical peptide reveals a rough energy landscape.  Biochemistry, 45 (30).  9068 - 9073.  ISSN 0006-2960     
relation: 10.1021/bi060858m