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
Easily polarizable N+H…N hydrogen bonds between histidine side chains and proton translocation in proteins
✍ Scribed by Pushti Prakash Rastogi; Wolfgang Kristof; Georg Zundel
- Book ID
- 118314749
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 310 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0006-291X
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## Synopsis The nature of hydrogen bonds formed between carboxylic acid residues and histidine residues in proteins is studied by ir spectroscopy. Poly(g1utamic acid) [(Glu),] is investigated with various monomer N bases. The position of the proton transfer equilibrium OH-N + O--H+N is determined
A 3D triple resonance experiment has been designed to provide intraresidual and sequential correlations between amide nitrogens and c~-carbons in uniformly 13C/15N-labeled proteins. In-phase 13C~ magnetization is transferred to the aliphatic side-chain protons via the side-chain carbons using a CC-T