Fluorine NMR studies of fluorocinnamoylchymotrypsins.

doi:10.1016/0003-9861(81)90267-8

Paper

Fluorine NMR studies of fluorocinnamoylchymotrypsins.

Published Jun 1, 1981 · J. T. Gerig, B. Halley

Archives of biochemistry and biophysics

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Abstract

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In Vitro Study

Study Snapshot

Fluorine NMR studies reveal that the presence of the fluorocinnamoyl group greatly stabilizes the enzyme towards denaturation in 8m urea.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Fluorine NMR studies of fluorocinnamoylchymotrypsins.

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References

NMR Studies of ortho and meta- fluorocinnamate-α-chymotrypsin complexes

Both o- and m-fluorocinnamate ions bind equally well to -chymotrypsin, with dipole-dipole interactions playing a key role in relaxing the protein-bound fluorine nucleus.

Expression of functionality of alpha-chymotrypsin. An alternate binding mode in the substrate specificity site.

Toluenesulfonamide and pipsylamide bind in alpha-chymotrypsin's substrate specificity site in a nonproductive manner, suggesting a potential new substrate-like binding mode.

Evidence for a structural change in the substrate preceding hydrolysis of a chymotrypsin acyl enzyme: application of the resonance Raman labelling technique to a dynamic biochemical system.

A structural change in the substrate occurs before deacylation of a chymotrypsin acyl enzyme, with the carbonyl group becoming more reactive.

Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding.

Dissociation of noncovalently bound inorganic phosphate from fluorotyrosine alkaline phosphatase is the rate-limiting process in enzyme catalysis at high pH.

Cryoenzymology of chymotrypsin: the detection of intermediates in the catalysis of a specific anilide substrate.

Subzero temperatures can reveal intermediates in enzyme mechanism studies, allowing for the accumulation of stable products at appropriate pH and low temperatures.

Deacylation of Fluorine-substituted trans-Cinnamoyl-α-chymotrypsins

P-methyl-substituted acylenzyme is more reactive than expected, while p-trifluoromethyl substitution results in a 10 times slower deacylation rate than expected.

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