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 β£-carbon, and the other on the amino acid sidechain. Geometry and energy parameters extracted from databank structures a
β¦ LIBER β¦
Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins
β Scribed by Tcherkasskaya, Olga; Ptitsyn, Oleg B.; Knutson, Jay R.
- Book ID
- 126158373
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 165 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-2960
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## Abstract The solvent accessibilities to the tryptophanyl microenvironments of wild type sperm whale apomyoglobin (apoMb) and two mutants (W7F and W14F) containing a single tryptophan are measured by fluorescence quenching studies. The results are compared to those relative to horse apoMb. In the