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- W2753697819 abstract "To conceive protein folding, a detailed knowledge about all thermodynamic states of proteins is required. The present work focuses on the characterization of the unfolded state ensemble. An experimental approach based on time-resolved FRET is employed, to characterize the conformations and dynamics of unfolded model peptides. The influence of temperature, viscosity and co-solutes is studied, to identify the speed limit of chain dynamics and to determine the forces that govern conformational transitions." @default.
- W2753697819 created "2017-09-15" @default.
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- W2753697819 date "2014-01-01" @default.
- W2753697819 modified "2023-09-27" @default.
- W2753697819 title "End-to-End Distance Distribution and Intra-Chain Diffusion in Unfolded Polypeptide Chains Determined by Time-Resolved FRET Measurements" @default.
- W2753697819 hasPublicationYear "2014" @default.
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