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Proton magnetic relaxation of proteins in the solid state: molecular dynamics of ribonuclease

✍ Scribed by E.R. Andrew; D.J. Bryant; E.M. Cashell

Publisher
Elsevier Science
Year
1980
Tongue
English
Weight
361 KB
Volume
69
Category
Article
ISSN
0009-2614

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✦ Synopsis

Measurements have been made of the proton NMR spin-lattice relaxation at 60,30 and 18 MHZ in solid ribonudwse A from IO to 300 K. and in a-chymotrypsin, lysozyme and deuterated lysozyme from 120 to 300 K. Reorientation of the methyl groups is the predominant moIecular motion causing relaxation. A lognormal distniution of correlation times best characterues the motions, with a spread of actwatron energies 14 t 6 kJ/mole.

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