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Energy landscape and dynamics of biomolecules: Extended abstract

Journal of Biological Physics (2005) 31(3-4) 413-416
DOI: 10.1007/s10867-005-0696-4
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Abstract

Proteins are not isolated homogeneous systems. Each protein can exist in a very large number of conformations (conformational substates) that are characterized by an energy landscape. The main conformational motions, similar to the α and β fluctuations in glasses, are linked to fluctuations in the bulk solvent and the hydration shell. © Springer 2005.

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Frauenfelder, H. (2005). Energy landscape and dynamics of biomolecules: Extended abstract. In Journal of Biological Physics (Vol. 31, pp. 413–416). https://doi.org/10.1007/s10867-005-0696-4

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