Algorithm for the systematic solvation of proteins based on the directionality of hydrogen bonds
β Scribed by Vedani, Angelo; Huhta, David W.
- Book ID
- 127245367
- Publisher
- American Chemical Society
- Year
- 1991
- Tongue
- English
- Weight
- 414 KB
- Volume
- 113
- Category
- Article
- ISSN
- 0002-7863
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π SIMILAR VOLUMES
The accessible minima in the electrostatic interaction energy of 29 bimolecular complexes containing N-H...O=C hydrogen bonds have been calculated, using ab initio distributed multipoles. The hydrogen bond geometries corresponding to these minima show the same statistical trends as found in crystal
Resorufm is shown to be a good probe solute for the direct measurement of the rates of formation and breaking of solventsolute hydrogen bonds. In ethanol, a hydrogen-bond equilibration time of 40 ps is found for both the ground and excited states. Deuteration of the solvent has no effect on the equi
Recently,l we investigated the possibility that NH.. .Sr(Cys) and NH.. .S\* hydrogen bonds (backbone amide NH, ligand sulfur) may help raise the redox potential of iron-sulfur proteins by differentially stabilizing the reduced (Cys-S)4Fe4S; cluster. By using molecular-orbital calculations on hydroge