Probing protein structure and dynamics by tritium NMR

✍ Scribed by T. M. O'Connell; P. G. Williams; J. T. Gerig

• Publisher: John Wiley and Sons
• Year: 1993
• Tongue: French
• Weight: 576 KB
• Volume: 33
• Category: Article
• ISSN: 0022-2135
• DOI: 10.1002/jlcr.2580330503

✦ Synopsis

Abstract

Tritium nmr spectroscopy of specifically tritiated tosylchymotrypsin has been used to examine the properties of the tosyl group in this protein. The unavoidable presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of relaxation behavior of tritiated species present were used in conjunction with models developed from crystallographic results to interpret the observations made. These analyses suggest that the tosyl group of tosylchymotrypsin at pH 4 is highly mobile in solution and occupies the lacation in the protein that is observed in the crystalline state only about 50% of the time.