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Circular dischroism and UV-resonance Raman investigation of the temperature dependence of the conformations of linear and cyclic elastin

Ahmed, Z and Scaffidi, JP and Asher, SA (2009) Circular dischroism and UV-resonance Raman investigation of the temperature dependence of the conformations of linear and cyclic elastin. Biopolymers, 91 (1). 52 - 60. ISSN 0006-3525

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Abstract

We used electronic circular dichroism (CD) and UV resonance Raman (UVRR) spectroscopy at 204 nm excitation to examine the temperature dependence of conformational changes in cyclic and linear elastin peptides. We utilize CD spectroscopy to study global conformation changes in elastin peptides, while UVRR is utilized to probe the local conformation and hydrogen bonding of Val and Pro peptide bonds. Our results indicate that at 20°C cyclic elastin predominantly populates distorted β-strand, β-type II and β-type III turn conformations. At 60°C, the β-type II turn population increases, while the distorted β-strand population decreases. Linear elastin predominantly adopts distorted β-strand and β-type III turn conformations with some β-type II turn population at 20°C. Increasing temperature to 60°C results in a small increase in the turn population. © 2008 Wiley Periodicals, Inc.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Ahmed, Z
Scaffidi, JP
Asher, SAasher@pitt.eduASHER
Date: 19 February 2009
Date Type: Publication
Journal or Publication Title: Biopolymers
Volume: 91
Number: 1
Page Range: 52 - 60
DOI or Unique Handle: 10.1002/bip.21081
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-3525
MeSH Headings: Circular Dichroism; Cyclization; Elastin--chemistry; Protein Conformation; Spectrum Analysis, Raman; Temperature
PubMed ID: 18932268
Date Deposited: 08 Feb 2013 20:50
Last Modified: 02 Feb 2019 16:55
URI: http://d-scholarship.pitt.edu/id/eprint/17261

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