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• W2110186295 startingPage "77" @default.
• W2110186295 abstract "Protein in water solution increases magnetic relaxation rates of solvent nuclei to an extent that depends on magnetic field strength and molecular weight. Koenig and Schillinger (J. Biol. Chem. 244, 3283 (1969)) showed that a small fraction of the water molecules in the first hydration shell, bound irrotationally with a residence lifetime in the range 01.1 to 10 us, would account for the phenomena. No experiments, as yet, have proven the existence of such long-lived waters, nor yielded a value for their lifetime. Analogous measurements on solutions of both denatured and cross-linked protein give data different from that of native protein, but much like results for tissue. By comparing proton and deuteron relaxation rates in solutions of native and cross-linked protein, it is possible to demonstrate the existence of these relatively long-lived waters; the data indicate that 1% of a monolayer of the waters of hydration of protein have lifetimes that cluster near 1 us and, it is argued, are held in place by multiple hydrogen bonds. Assigning shorter lifetimes for waters held by fewer bonds, it is possible to develop a unified view of relaxation of water nuclei in protein solutions and in tissue, and to relate it to recent crystallographic data on hydrated protein." @default.
• W2110186295 created "2016-06-24" @default.
• W2110186295 creator A5022650078 @default.
• W2110186295 creator A5028326396 @default.
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• W2110186295 date "1993-01-01" @default.
• W2110186295 modified "2023-10-16" @default.
• W2110186295 title "A unified view of relaxation in protein solutions and tissue, including hydration and magnetization transfer" @default.
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• W2110186295 doi "https://doi.org/10.1002/mrm.1910290114" @default.
• W2110186295 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8380481" @default.
• W2110186295 hasPublicationYear "1993" @default.
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