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Effect of temperature on the spin-lattice relaxation times of aqueous solutions of ribonuclease and human serum albumin

✍ Scribed by D. J. Blears; S. S. Danyluk

Publisher
Wiley (John Wiley & Sons)
Year
1965
Tongue
English
Weight
328 KB
Volume
3
Category
Article
ISSN
0006-3525

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✦ Synopsis

Aqueous solutions of ribonuclease and human serum albumin were subjected to periods of controlled heating and the nuclear magnetic spin-lattice relaxation times, 2'1, of the water protons measured. The heat treatment causes an initial increase in the relaxation times of the water protons. These TI variations indicate that a configurational change, compatible with a disordering of the protein structure occurs, which involves an increase in various modes of internal mobility. The TI measurements also indicate a close, ordered association of the wat,er molecules and the protein.

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