Effective van der Waals radii were calibrated in such a way that molecular models built from standard bond lengths and bond angles reproduced the amino acid conformations observed by crystallography in proteins and peptides. The calibrations were based on the comparison of the Ramachandran plots pre
โฆ LIBER โฆ
Optimization of van der Waals Energy for Protein Side-Chain Placement and Design
โ Scribed by Fahmy, Amr; Wagner, Gerhard
- Book ID
- 119209079
- Publisher
- Biophysical Society
- Year
- 2011
- Tongue
- English
- Weight
- 406 KB
- Volume
- 101
- Category
- Article
- ISSN
- 0006-3495
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