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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?
References:
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 |
