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. 1972 Mar;69(3):599–602. doi: 10.1073/pnas.69.3.599

Proton Nuclear Magnetic Resonance Studies of Ribonuclease A in H2O

Dinshaw J Patel *, Clare K Woodward †, Frank A Bovey *
PMCID: PMC426515  PMID: 4501576

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°. 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.

Keywords: histidine, NMR exchangeable protons

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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