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Default Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectrosc

Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectroscopy.

Related Articles Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectroscopy.

Biochim Biophys Acta. 1994 Sep 21;1208(1):171-8

Authors: O'Connell TM, Gerig JT, Williams PG

3H-NMR spectroscopy of specifically tritiated and tritiated/deuterated derivatives of tosylchymotrypsin has been used to examine the behavior of the tosyl group in this protein at pH 7. The presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of T1 relaxation, line widths, and various nuclear Overhauser experiments for the collection of tritiated species present in the samples were used to the interpret the observations made. These analyses suggests that the tosyl group of tosylchymotrypsin at pH 7 is largely retained within the substrate specificity pocket observed in the crystal structure. This outcome is in strong contrast to the situation observed at pH 4, where the tosyl group is mobile enough to be found outside the specificity pocket an appreciable fraction of the time, and may be the result of protein association at pH 7.

PMID: 8086432 [PubMed - indexed for MEDLINE]



Source: PubMed
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