(Georgia Institute of Technology, 1996)
Vieth, Michal; Kolinski, Andrzej; Brooks, C. L., III; Skolnick, Jeffrey
A hierarchical approach to protein folding is employed to examine the folding pathway and predict the quaternary structure of the GCN4 leucine zipper. Structures comparable in quality to experiment have been predicted. In addition, the equilibrium between dimers, trimers and tetramers of a number of GCN4 mutants has been examined. In five out of eight cases, the simulation results are in accordance with the experimental studies of Harbury, et al.
(Georgia Institute of Technology, 1995)
Milik, Mariusz; Skolnick, Jeffrey
A system is presented for generating peptide sequences with desirable properties,
using combination of neural network and artificial evolution. The
process is illustrated by an example of a practical problem of generating
artificial transbilayer peptides. The peptides generated in the process of
artificial evolution have the physico-chemical properties of transmembrane
peptides, and forms stable transmembrane structures in testing Monte Carlo
simulations. The artificial evolution system is designed to emulate natural
evolution; therefore it is of both practical and theoretical interest, both in
terms of rational design of protein sequences and modeling of natural evolution
of proteins.