Premium
Recent progress in the theoretical treatment of protein folding
Author(s) -
Scheraga Harold A.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220104
Subject(s) - chemistry , melittin , globular protein , amino acid residue , maxima and minima , residue (chemistry) , protein folding , energy minimization , biophysics , peptide , computational chemistry , biochemistry , peptide sequence , mathematical analysis , mathematics , biology , gene
The multiple‐minima problem encountered in computations of the conformational energy of a globular protein can be approached by extending, in part, the methodology used heretofore to treat small oligopeptides and fibrous proteins, and by incorporating procedures to treat short‐, medium, and long‐range interactions. The latter consist primarily of energy minimization and application of distance constraints. Initial tests with the 20‐residue membrane‐bound portion of melittin and with the 58‐residue bovine pancreatic trypsin inhibitor are sufficiently encouraging to suggest that the potential functions and computational algorithms are reasonable and extendable to globular proteins containing as many as 200 amino acid residues.