NMR, alcohols, protein solvation and protein denaturation.
The amino acid side chains of Ser, Thr and Tyr contain the hydroxyl functional group that is characteristic of alcohols, and a variety of different alcohols are used either as structure-inducing or denaturing co-solvents in physical-chemical studies of proteins. This article surveys selected aspects of the influence of protein-intrinsic and -extrinsic hydroxyl groups on studies of the solvation of peptides and proteins by nuclear magnetic resonance (NMR) spectroscopy.
Wüthrich
K
K
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
D000438:Alcohols; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D012694:Serine; D012997:Solvents; D013912:Threonine; D014443:Tyrosine
D000438:Alcohols; D011506:Proteins; D012997:Solvents; D013912:Threonine; D014443:Tyrosine; D012694:Serine