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UV Raman studies of peptide conformation demonstrate that betanova does not cooperatively unfold

Boyden, MN and Asher, SA (2001) UV Raman studies of peptide conformation demonstrate that betanova does not cooperatively unfold. Biochemistry, 40 (45). 13723 - 13727. ISSN 0006-2960

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We used UV resonance Raman spectroscopy (UVRR) excited within the peptide bond π→π*electronic transitions and within the aromatic amino acid π→π*electronic transitions to examine the temperature dependence of the solution conformation of betanova, a 20-residue β-sheet polypeptide [Kortemme, T., Ramirez-Alvarado, M., and Serrano, L. (1998) Science 281, 253-256]. The 206.5 nm excited UVRR enhances the amide vibrations and demonstrates that betanova has a predominantly β-sheet structure between 5 and 82 °C. The 229 nm excited UVRR, which probes the tyrosine and tryptophan side chain vibrations, shows an increase in the solvent exposure of the tryptophan side chains as the temperature is increased. Our results are consistent with the existence of an intermediate state similar to that calculated by Bursulaya and Brooks [Bursulaya, B. D., and Brooks, C. L. (1999) J. Am. Chem. Soc. 121, 9947-9951] and exclude the previously proposed two-state cooperative folding mechanism. Betanova's structure appears to be molten globule over the 3-82 °C temperature range of our study.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Boyden, MN
Asher, SAasher@pitt.eduASHER
Date: 13 November 2001
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 40
Number: 45
Page Range: 13723 - 13727
DOI or Unique Handle: 10.1021/bi011505k
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: Circular Dichroism; Peptides--chemistry; Protein Folding; Protein Structure, Secondary; Proteins--chemistry; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman--methods
PubMed ID: 11695921
Date Deposited: 20 Mar 2013 16:43
Last Modified: 02 Feb 2019 16:55


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