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Diffuse scattering in protein crystallography

Published online by Cambridge University Press:  17 March 2009

Jean-Pierre Benoit  and
Jean Doucet
Jean-Pierre Benoit
Affiliation:
Laboratoire d'Utilisation du Ravonnement Electromagnétique, Bât. 209D, Universite Paris-Sud, F-91405, Orsay Cedex, France
Jean Doucet
Affiliation:
Laboratoire d'Utilisation du Ravonnement Electromagnétique, Bât. 209D, Universite Paris-Sud, F-91405, Orsay Cedex, France Laboratoire d'Utilisation du Ravonnement Electromagnétique, Bât. 209D, Universite Paris-Sud, F-91405, Orsay Cedex, France
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Extract

The understanding of flexibility and deformability in proteins is one of the current major challenges of structural molecular biology. The knowledge of the average atomic positions of three-dimensional folding of proteins, which is obtained either by X-ray diffraction or n.m.r. spectroscopy, is generally not sufficient to explain their functional mechanisms. Very often it is necessary to consider the existence of other concerted atomic motions as, for example, in the well-known case of the CO molecule fixation at the active site of myoglobin which requires the concerted displacement of a large number of atoms in order to open a channel down to this site. This opening, which depends on the physico-chemical conditions, plays the role of a regulator in the biochemical reactions (Janin & Wodak, 1983; Tainer et al. 1984; Westhof et al. 1984; Ormos et al. 1988).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 28 , Issue 2 , May 1995 , pp. 131 - 169
Copyright
Copyright © Cambridge University Press 1995

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