Assignment of the imidazole ring nitrogen protons of histidine 48 in the proton NMR spectrum of ribonuclease A in water solution
โ Scribed by Dinshaw J. Patel; Lita L. Canuel; Frank A. Bovey; Clare Woodward
- Book ID
- 113124881
- Publisher
- Elsevier Science
- Year
- 1975
- Weight
- 410 KB
- Volume
- 400
- Category
- Article
- ISSN
- 0005-2795
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## Synopsis Described herein are proton nmr experiments on chemically modified derivatives of riboniiclease A designed to elucidate the origin of an exchangeable resonance, assigned previously to a histidine ring N proton that titrates between 11 to 13 ppm with a pK, of 6.1 in HzO solution. Histid
The assignment of two histidine proton resonances in the proton NMR spectrum of ribonuclease A has been made by forming a paramagnetic complex between pentaammineruthenium(II1) and the N-3 nitrogen of a single histidine residue. Reaction of chloropentaammineruthenium(III)dichloride with ribonuclease
The ionization characteristics of the hydrogen-bonded His 12 AT1 proton observed to titrate between 11 to 13 ppm in the nnir spectrum of ribonuclease A in He0 solution are compared with the ionization characteristics of the four histidine CZ protons in the enzyme. Comparison of the pK,'s of the enzy