NMR study of internal hydrogen bonds in metalloproteins

摘要: Abstract The NMR characterization of the structure function relationship in metalloproteins using high frequency shifted His imidazole ring NH proton signals as spectroscopic probes are reviewed, with examples studies myoglobin, cytochrome c, and superoxide dismutase. residues often found active site a variety enzymes proton-donor or -acceptor forming internal hydrogen bonds, which contribute to stabilization protein folding. Since that participates an bond within matrix is magnetically deshielded exhibits moderate exchange rate, its signal resolved outside envelope, 0–10 ppm. These highly sensitive electronic microenvironments unequivocally describe tautomerism protonation behaviour side-chains. parameters hydrogen-bonded reflect strength local tertiary therefore provide unique structural information cannot be obtained by other techniques.