Hydrogen bonds involving sulfur atoms in proteins
✍ Scribed by Lydia M. Gregoret; Stephen D. Rader; Robert J. Fletterick; Fred E. Cohen
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 694 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
Intrachain hydrogen bonds are a hallmark of globular proteins. Traditionally, these involve oxygen and nitrogen atoms. The electronic structure of sulfur is compatible with hydrogen bond formation as well. We surveyed a set of 85 high-resolution protein structures in order to evaluate the prevalence and geometry of sulfur-containing hydrogen bonds. This information should be of interest to experimentalists and theoreticians interested in protein structure and protein engineering.
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The intermolecular stretching vibration of hydrogen bonded complexes between phenol derivatives and tetramethylthiourea or dimethylthioformamide is observed in the range 113 -131 cm-'. The corresponding force constants ko are computed using the Lippincott-Schroeder potential function and the matrix
## Abstract The PCILO method was used to study systems with the following types of intermolecular hydrogen bonds, involving 2nd row atoms: N…︁HS, S…︁HS, N…︁HCl, Cl…︁HF, Cl…︁HCl, P…︁HN, P…︁HP, P…︁HF, S…︁HF. In all the cases calculated, the PCILO method yields an accurate qualitative descri