High Resolution Nuclear Magnetic Resonance Study of the Histidine-Aspartate Hydrogen Bond in Chymotrypsin and Chymotrypsinogen

George Robillard, R.G. Shulman

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Abstract

A high resolution proton nuclear magnetic resonance study of chymotrypsin Aδ and chymotrypsinogen A in water has shown a single resonance at very low magnetic fields (-18 to -15 p.p.m. relative to dimethyl-silapentane-sulfonate). From its pH dependence (pK = 7.2) and response to chemical modification the resonance has been assigned to the hydrogen-bonded proton between His-57 and Asp-102.
Original languageEnglish
Number of pages5
JournalJournal of Molecular Biology
Volume71
Issue number2
DOIs
Publication statusPublished - 1972

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