Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for site-specific assignments of carbons nearby labile protein protons. We compare the proton T2' selective scheme to frequency selective water observation in deuterated proteins, and discuss the impacts of deuteration on 13C linewidths in Crh. We observe that in micro-crystalline proteins, solvent accessible hydroxyl and amino protons show comparable exchange rates with water protons as for proteins in solution, and that structural constraints, such as hydrogen bonding or solvent accessibility, more significantly reduce exchange rates.
Böckmann
Anja
A
BioSciences Lyon-Gerland, Institut de Biologie et Chimie des Protéines UMR 5086 CNRS/ULCB, 7, passage du Vercors, 69367, Lyon, France. a.bockmann@ibcp.fr
Juy
Michel
M
Bettler
Emmanuel
E
Emsley
Lyndon
L
Galinier
Anne
A
Penin
François
F
Lesage
Anne
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D003903:Deuterium; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry*; D011487:Protein Conformation; D014867:Water
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D014867:Water; D006859:Hydrogen; D003903:Deuterium; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr