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Structural effects of hydration: Studies of lysozyme by 13 C solids nmr
Author(s) -
Kennedy Scott D.,
Bryant Robert G.
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360291411
Subject(s) - chemistry , lysozyme , magic angle spinning , dipole , nmr spectra database , magnetization transfer , spectral line , proton , magnetic dipole–dipole interaction , magic angle , nuclear magnetic resonance , relaxation (psychology) , crystallography , magnetization , nuclear magnetic resonance spectroscopy , analytical chemistry (journal) , stereochemistry , magnetic field , organic chemistry , medicine , psychology , social psychology , biochemistry , physics , quantum mechanics , astronomy , magnetic resonance imaging , radiology
13 C‐nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic‐angle‐spinning‐cross‐polarization methods are reported at several water contents. The line widths and consequent resolution in the hydrated material is substantially improved over that in the lyophilized protein. The line narrowing is not commensurate with loss of a proton–carbon dipole–dipole coupling or dramatic changes in the relaxation parameters characterizing magnetization transfer from protons to carbon in the Hartmann–Hahn cross‐polarization experiment. We interpret these data in terms of the water inducing a decrease in the conformational reorientations required to account for the data are not necessarily large nor do they imply a major unfolding of the protein on dehydration.