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Carbon-13 nuclear magnetic resonance relaxation study of chymotrypsin inhibitor 2 (CI-2)

✍ Scribed by Robin J. Leatherbarrow; Stephen J. Matthews

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
555 KB
Volume
30
Category
Article
ISSN
0749-1581

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✦ Synopsis

Abstract

Carbon‐13 T~1~ and NOE measurements were used to study the internal motions of the single phenylalanine residue in CI‐2 and in a mutant in which an arginine residue adjacent to the Phe had been replaced with an alanine residue. Each protein was specifically enriched with [^13^C~6~‐ring]phenylalanine. The arginine to alanine modification resulted in a reduction of the order parameter, S^2^, from 0.39 to 0.32 for the internal motions of the aromatic ring. This is consistent with the aromatic side‐chain of Phe 69 being less restricted, as a consequence of the removal of the neighbouring bulky side chain. Wild‐type CI‐2 was also successfully enriched with [2‐^13^C]glycine. An average order parameter of 0.60 was obtained for the α‐carbon positions of the three glycine residues. When bound to the serine protease chymotrypsin, S^2^ remains unchanged within experimental error. However, the overall tumbling, derived from NMR, slows by a factor of 5, consistent with the increase in molecular weight.

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