A coarse-grained dynamic Monte Carlo method is proposed for investigating the conformational dynamics of proteins. Each residue is represented by two interaction sites, one at the ␣-carbon, and the other on the amino acid sidechain. Geometry and energy parameters extracted from databank structures a
Coarse-grained simulations of the conformational dynamics of proteins
✍ Scribed by T. Haliloğlu
- Book ID
- 108487062
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 195 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1089-3156
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A coarse-grained dynamic Monte Carlo (MC) simulation method is used to investigate the conformational dynamics of chymotrypsin inhibitor 2 (CI2). Each residue is represented therein by two interaction sites, one at the ␣-carbon and the other on the amino acid side-chain. The energy and geometry para
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