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UV resonance Raman investigation of a 3<inf>10</inf>-helical peptide reveals a rough energy landscape

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

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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.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Ahmed, Z
Asher, SAasher@pitt.eduASHER
Date: 1 August 2006
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 45
Number: 30
Page Range: 9068 - 9073
DOI or Unique Handle: 10.1021/bi060858m
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: HIV Envelope Protein gp41--chemistry; Peptide Fragments--chemistry; Protein Conformation; Protein Structure, Secondary; Spectrophotometry, Ultraviolet--methods; Spectrum Analysis, Raman--methods; Temperature; Thermodynamics
PubMed ID: 16866352
Date Deposited: 08 Feb 2013 21:11
Last Modified: 22 Jun 2021 13:55


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