J. Chim. Phys.
Volume 88, 1991
|Page(s)||2522 - 2522|
|Published online||29 May 2017|
The multiple-minima problem in protein folding
Cornell University, Ithaca, New York 14853-1301, USA.
The conformational energy surface of a polypeptide or protein has many local minima, and conventional energy minimization procedures reach only a local minimum (near the starting point of the optimization algorithm) instead of the global minimum (the multiple-minima problem). Several procedures have been developed to surmount this problem, the most promising of which are:
build up procedure,
optimization of electrostatics,
Monte Carlo plus minimization,
electrostatically driven Monte Carlo,
inclusion of distance restraints,
adaptive importance sampling Monte Carlo
relaxation of dimensionality,
pattern recognition, and
diffusion equation method.
These procedures have been applied to a variety of polypeptide structural problems, and the results of such computations will be presented. These include the computation of the structures of open-chain and cyclic peptides, fibrous proteins and globular proteins. Present efforts are being devoted to scaling up these procedures from small polypeptides to proteins, to try to compute the three-dimensional structure of a protein from its amino sequence.
© Elsevier, Paris, 1991