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UV resonance Raman study of the spatial dependence of α-helix unfolding

Ianoul, A and Mikhonin, A and Lednev, IK and Asher, SA (2002) UV resonance Raman study of the spatial dependence of α-helix unfolding. Journal of Physical Chemistry A, 106 (14). 3621 - 3624. ISSN 1089-5639

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We used ultraviolet resonance Raman (UVRR) spectra to examine the spatial dependence and the thermodynamics of α-helix melting of an isotopically labeled α-helical, 21-residue, mainly alanine peptide. The peptide was synthesized with six natural abundance amino acids at the center and mainly perdeuterated residues elsewhere. Cα deuteration of a peptide bond decouples Cα-H bending from N-H bending, which significantly shifts the random coil conformation amide III band; this shift clearly resolves it from the amide III band of the nondeuterated peptide bonds. Analysis of the isotopically spectrally resolved amide III bands from the external and central peptide amide bonds show that the six central amide bonds have a higher α-helix melting temperature (∼32°C) than that of the exterior amide bonds (∼5°C).


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Ianoul, A
Mikhonin, A
Lednev, IK
Asher, SAasher@pitt.eduASHER
Date: 11 April 2002
Date Type: Publication
Journal or Publication Title: Journal of Physical Chemistry A
Volume: 106
Number: 14
Page Range: 3621 - 3624
DOI or Unique Handle: 10.1021/jp013537n
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1089-5639
Date Deposited: 27 Feb 2013 18:48
Last Modified: 22 Jun 2021 13:55


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