Circular dichroism and UV‐resonance Raman investigation of the temperature dependence of the conformations of linear and cyclic elastin

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. Biopolymers 91: 52–60, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com