ISSN:
0887-3585
Keywords:
overdamped langevin dynamics
;
thermal motion
;
neurotrophin
;
glutamine synthetase
;
atomic displacement parameter
;
x-ray diffraction data
;
loop mobility
;
disorder
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
In the course of refining atomic protein structures, one often encounters difficulty with molecules that are unusually flexible or otherwise disordered. We approach the problem by combining two relatively recent developments: simultaneous refinement of multiple protein conformations and highly constrained refinement. A constrained Langevin dynamics refinement is tested on two proteins: neurotrophin-3 and glutamine synthetase. The method produces closer agreement between the calculated and observed scattering amplitudes than standard, single-copy, Gaussian atomic displacement parameter refinement. This is accomplished without significantly increasing the number of fitting parameters in the model. These results suggest that loop motion in proteins within a crystal lattice can be extensive and that it is poorly modeled by isotropic Gaussian distributions for each atom. Proteins 29:426-432, 1997. © 1997 Wiley-Liss, Inc.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
