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Proton Nuclear Magnetic Resonance Studies of Ribonuclease A in H2O

Dinshaw J. Patel, Clare K. Woodward and Frank A. Bovey
Proceedings of the National Academy of Sciences of the United States of America
Vol. 69, No. 3 (Mar., 1972), pp. 599-602
Stable URL: http://www.jstor.org/stable/61338
Page Count: 4
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Proton Nuclear Magnetic Resonance Studies of Ribonuclease A in H2O
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Abstract

A resonance (designated a) due to an exchangeable proton titrates (pKa = 6.1) between 11.5 and 13 ppm in the nuclear magnetic resonance spectrum of RNase A-0.2 M NaCl in H2O at 20 degrees. Comparison with models has permitted assignment to a ring-nitrogen proton of histidine in slow exchange with solvent H2O. The pH and temperature-dependent line-width changes of resonance a are analyzed in terms of an exchange between histidine and protonated histidine, without the necessity to invoke any exchange processes associated with protein conformational changes. Several other resonances due to exchangeable protons are observed between 10 and 15 ppm in the nuclear magnetic resonance spectrum of RNase A in H2O.

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