proccss '' kilns. Ti1 otlicr words, tlic licnt hi gnscs a t nhoiit 900' C. is iiiorc cnicicntly iitiliscd tlinti tlic siitiic ntiioant of licnt in t1oul)lc tlic quantity of gnses at, say, 500Β° C. Still, wnstclirnt, r c c o \ -t ~~\* hoilcrs arc in successful illid protitnblc opcrntioti with tlic cnt
Recent progress in the theoretical treatment of protein folding
β Scribed by Harold A. Scheraga
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 814 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ 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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We numerically compare the effectiveness of three recently proposed algorithms, multicanonical algorithm, simulations in a 1rk-sampling, and simulated tempering, for the protein folding problem. We perform simulations with high statistics for one of the simplest peptides, met-enkephalin. While the p