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Recent progress in the theoretical treatment of protein folding

✍ Scribed by Harold A. Scheraga


Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
814 KB
Volume
22
Category
Article
ISSN
0006-3525

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✦ Synopsis


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.


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