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Molecular Biophysics  


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An extremely interesting observation made in our studies of structural dynamics in the last decade is the close correlation between the conformational fluctuations that are predicted to be most easily accessible under native state conditions and the structural changes experimentally observed in different functional forms of a given protein. In summary,

(1) each structure encodes a unique dynamic. Structure-encoded motions are predominantly defined by the inter-residue contact topology, and may be readily elucidated by elastic network models normal mode analysis.

(2) structure-encoded motions are functional. For example, the exposure or closing of an enzyme catalytic cleft, gating of an ion/substrate channel, processing of substrate, etc. involve collective domain movements that are intrinsically favored by the 3-d network of non-bonded contacts.


    Do these results imply that structures are evolutionarily selected to perform functional dynamics?

Ponzoni, L Zhang, S, Cheng, MH, Bahar, I. (2018) Shared Dynamics of LeuT Superfamily Members and Allosteric Differentiation by Structural Irregularities and Multimerization. Philos Trans R Soc Lond B Biol Sci, in press