𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Displaying hydrogen bonds in proteins involving side chain atoms

✍ Scribed by Khaled Belhadj-Mostefa; Ron Poet; E.James Milner-White

Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
125 KB
Volume
11
Category
Article
ISSN
0263-7855

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Hydrogen bonds involving sulfur atoms in
Hydrogen bonds involving sulfur atoms in proteins
✍ Lydia M. Gregoret; Stephen D. Rader; Robert J. Fletterick; Fred E. Cohen πŸ“‚ Article πŸ“… 1991 πŸ› John Wiley and Sons 🌐 English βš– 694 KB

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

Side chain–backbone hydrogen bonds in pe
Side chain–backbone hydrogen bonds in peptides containing glutamic acid residues
✍ Roger Mayer; GΓ©rard Lancelot; GΓ©rard Spach πŸ“‚ Article πŸ“… 1979 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 181 KB πŸ‘ 2 views

Over the last few years x-ray diffraction and nmr investigations have been reported for a variety of natural and synthetic peptides in order to enhance our understanding of the conformation of several amino acid side chains and especially those bearing functional groups such as hydroxyl, sulfhydryl,

Structurally symmetrical, easily polariz
Structurally symmetrical, easily polarizable hydrogen bonds between side chains in proteins and proton-conducting mechanisms. III
✍ Wolfgang Kristof; Georg Zundel πŸ“‚ Article πŸ“… 1980 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 839 KB

Republic of Germany synopsis (L-Cys),, (L-LYS),, and (L-G~u), were studied by ir spectroscopy in terms of their degree of deprotonation or protonation. It is shown that structurally symmetrical, easily polarizable SH-S-+ -S--HS, N+H-N =N.--H+N, and OH---0-\* -0-HO hydrogen bonds are formed between t