International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 18.2, p. 378
Figure 18.2.4.1
a
The Howard Hughes Medical Institute, and Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, and Stanford Synchrotron Radiation Laboratory, Stanford Universty, 1201 Welch Road, MSLS P210, Stanford, CA 94305-5489, USA,bThe Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA, and cDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA |
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Figure 18.2.4.1
Illustration of simulated annealing for minimization of a one-dimensional function. The kinetic energy of the system (a `ball' rolling on the one-dimensional surface) allows local conformational transitions with barriers smaller than the kinetic energy. If a larger drop in energy is encountered, the excess kinetic energy is dissipated. It is thus unlikely that the system can climb out of the global minimum once it has reached it. |