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• W2068220314 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." @default.
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• W2068220314 date "2007-06-14" @default.
• W2068220314 modified "2023-10-17" @default.
• W2068220314 title "Temperature-Induced Conformational Transition of a Model Elastin-like Peptide GVG(VPGVG)₃ in Water" @default.
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• W2068220314 doi "https://doi.org/10.1021/bm070233j" @default.
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