The fact that protein structures are dynamic by nature and that structure models determined by X-ray crystallography, electron microscopy (EM) and nuclear magnetic resonance (NMR) spectroscopy have limited accuracy limits the precision with which derived properties can be reported. Here, the issue o
Pairwise calculation of protein solvent-accessible surface areas
β Scribed by Arthur G. Street; Stephen L. Mayo
- Book ID
- 114382700
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 90 KB
- Volume
- 3
- Category
- Article
- ISSN
- 1359-0278
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We explored the use of several breadth-first and depth-first algorithms for the computation of Gaussian atomic and molecular surface areas. Ε½ . Our results for whole-molecule van der Waals surface areas vdWSAs were 10 times more accurate in relative error, relative to actual hard-sphere areas, than
A fast analytical formula (TDND) has been derived for the calculation of approximate atomic and molecular solvent-accessible surface areas (SASA), as well as the first and second derivatives of these quantities with respect to atomic coordinates. Extending the work of Stouten et al. (Molecular Simul