title: Temperature-induced conformational transition of a model elastin-like peptide GVG(VPGVG)(3) in water.
abstract: The conformation of a single elastin-like peptide GVG(VPGVG)3 in liquid water is studied by computer simulations in the temperature interval between 280 and 440 K. Two main conformational states of the peptide can be distinguished: a rigid conformational state, dominating at low temperatures, and a flexible conformational state, dominating at high temperatures. A temperature-induced transition between these states occurs at about 310 K, rather close to a transition temperature seen in experiments. This transition is accompanied by the thermal breaking of the hydrogen-bonded spanning network of the hydration water via a percolation transition upon heating. This finding indicates that the H-bond clustering structure of the hydration water plays an important role in the conformational stability of biomolecules. A second important observation is the Gaussian distribution of the end-to-end distance in the high-temperature state, which supports the idea of a rubber-like elasticity of the studied elastin-like peptide. Finally our results challenge the idea of the folding of elastin-like peptides upon heating.
authors.affiliation: Physical Chemistry, University of Dortmund, Dortmund D-44221, Germany.
authors.forename: Aliaksei
authors.initials: A
authors.lastname: Krukau
authors.forename: Ivan
authors.initials: I
authors.lastname: Brovchenko
authors.forename: Alfons
authors.initials: A
authors.lastname: Geiger
mesh_terms: D004549:Elastin / Q000737:chemistry*; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry*; D011336:Probability; D013696:Temperature
chemical_list: D010455:Peptides; D004549:Elastin