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Biophys J, March 2001, p. 1115-1123, Vol. 80, No. 3

Protein Flexibility from the Dynamical Transition: A Force Constant Analysis

D. J. Bicout*dagger and G. Zaccaidagger Dagger

 *INFM-Operative Group Grenoble CRG IN13 and  dagger Institut Laue-Langevin, 38042 Grenoble Cedex 9, France; and  Dagger Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, F-38027 Grenoble Cedex 1, France

A standard analysis of the scattered neutron incoherent elastic intensity measured with very good energy resolution yields elastic scans, i.e., mean-square displacements of atomic motions (in a pico to nanosecond time scale) in a sample as a function of temperature. This provides a quick way for characterizing the dynamical behavior of biological macromolecules, such behavior being correlated with biological function and activity. Elastic scans of proteins exhibit a dynamical transition at ~200 K, marking a cross-over in molecular fluctuations between harmonic and nonharmonic dynamical regimes. This paper presents an approach allowing analysis of the elastic scan in terms of force constants and related parameters, such as the free energy barrier Delta G at the transition. We find that the increased protein flexibility beyond the dynamical transition is associated with Delta G ~ RT and effective force constants of the order of 0.1-3 N/m. The analysis provides a set of parameters for characterizing molecular resilience and exploring relations among dynamics, function, and activity in proteins.

Biophys J, March 2001, p. 1115-1123, Vol. 80, No. 3
© 2001 by the Biophysical Society   0006-3495/01/03/1115/09  $2.00


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