Issue |
J. Chim. Phys.
Volume 88, 1991
|
|
---|---|---|
Page(s) | 2522 - 2522 | |
DOI | https://doi.org/10.1051/jcp/1991882522 | |
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:
- (a)
build up procedure,
-
(b)
optimization of electrostatics,
- (c)
Monte Carlo plus minimization,
-
(d)
electrostatically driven Monte Carlo,
-
(e)
inclusion of distance restraints,
-
(f)
adaptive importance sampling Monte Carlo
- (g)
relaxation of dimensionality,
- (h)
pattern recognition, and
- (i)
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