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
New dimension indices for the characterization of the solvent-accessible surface
✍ Scribed by Francisco Torrens; José Sánchez–Marín; Ignacio Nebot–Gil
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 250 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0192-8651
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## Abstract In the calculation of thermodynamic properties and three‐dimensional structures of macromolecules, such as proteins, it is important to have an efficient algorithm for computing the solvent‐accessible surface area of macromolecules. Here, we propose a new analytical method for this purp
## Abstract Predicting the solvent accessible surface area (ASA) of transmembrane (TM) residues is of great importance for experimental researchers to elucidate diverse physiological processes. TM residues fall into two major structural classes (α‐helix membrane protein and β‐barrel membrane protei
An algorithm is presented for calculating the solvent accessible surface area of proteins using a threedimensional grid. Since it requires only calculations based on single atomic positions, the algorithm is easy to be vectorized. It has been implemented on STlOO and may also be implemented on super