Temperature-Induced Collapse of Elastin-like Peptides Studied by 2DIR Spectroscopy.

ABSTRACT: Elastin-like peptides are hydrophobic biopolymers that exhibit a reversible coacervation transition when the temperature is raised above a critical point. Here, we use a combination of linear infrared spectroscopy, two-dimensional infrared spectroscopy, and molecular dynamics simulations to study the structural dynamics of two elastin-like peptides. Specifically, we investigate the effect of the solvent environment and temperature on the structural dynamics of a short (5-residue) elastin-like peptide and of a long (450-residue) elastin-like peptide. We identify two vibrational energy transfer processes that take place within the amide I' band of both peptides. We observe that the rate constant of one of the exchange processes is strongly dependent on the solvent environment and argue that

SUBMITTER: Selig O 

PROVIDER: S-EPMC6143280 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature