Two efficient algorithms have been developed which allow amino acid side chain
conformations to be optimized rapidly for a given peptide backbone conformation. Both …

Methods for describing a discrete number of conformational states of amino acid residues in
proteins are presented and used to investigate the topography of chain folding. The relative …

Revised Manuscript Received June 12, 1992 abstract: A recently developed procedure to
predict backbone structure from the amino acid sequence [Rooman, M., Kocher, JP, & …

The feasibility of determining the conformation of segments of a polypeptide chain up to six
residues in length in globular proteins by means of a systematic search through the possible …

A backbone-dependent rotamer library for amino acid side-chains is developed and used for
constructing protein side-chain conformations from the main-chain co-ordinates. The …

A procedure, CONGEN, for uniformly sampling the conformational spaceof short polypeptide
segments in proteins has been implemented. Because thetime required for this sampling …

A method is developed to compute backbone tertiary folds from the amino acid sequence. In
this method, the number of degrees of freedom is drastically reduced by neglecting side …

Two principal methods of determining the conformation of short pieces of polypeptide
backbone in proteins have been developed: using a database of known structures and …

We have developed a computational method for accurately predicting the conformation of
side-chain atoms when building a protein structure from a known homologous structure. A …

The build‐up procedure for predicting low‐energy conformations of polypeptides has been
extended to cover the case of peptides in aqueous solutions. The revised procedure …