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UV raman examination of α-helical peptide water hydrogen bonding

Pimenov, KV and Bykov, SV and Mikhonin, AV and Asher, SA (2005) UV raman examination of α-helical peptide water hydrogen bonding. Journal of the American Chemical Society, 127 (9). 2840 - 2841. ISSN 0002-7863

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UV resonance Raman spectra (UVRS) of an α-helical, 21 residue, mainly Ala peptide (AP) in the dehydrated solid state were compared to those in aqueous solution at different temperatures. The UVRS amide band frequencies of a dehydrated solid α-helix peptide show frequency shifts compared to those in aqueous solution due to the loss of amide backbone hydrogen bonding to water; the amide II and amide III bands of the solid α-helix downshift, while the amide I band upshifts. The shifts are identical in direction but smaller than those that occur for α-helices in aqueous solution as the temperature increases; water hydrogen bonding strengths decrease as the temperature increases. The UV Raman amide band frequency shifts can be used to monitor α-helix hydrogen bonding. Copyright © 2005 American Chemical Society.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Pimenov, KV
Bykov, SV
Mikhonin, AV
Asher, SAasher@pitt.eduASHER
Date: 9 March 2005
Date Type: Publication
Journal or Publication Title: Journal of the American Chemical Society
Volume: 127
Number: 9
Page Range: 2840 - 2841
DOI or Unique Handle: 10.1021/ja044708f
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0002-7863
MeSH Headings: Cold Temperature; Hot Temperature; Hydrogen Bonding; Kinetics; Peptides--chemistry; Polyglutamic Acid--chemistry; Polylysine--chemistry; Protein Structure, Secondary; Spectrophotometry, Ultraviolet--methods; Spectrum Analysis, Raman--methods; Water--chemistry
PubMed ID: 15740105
Date Deposited: 08 Feb 2013 21:20
Last Modified: 02 Feb 2019 15:59


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