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Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to α-chymotrypsin

Gammon, Kenneth L. and Smallcombe, Stephen H. and Richards, John H. (1972) Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to α-chymotrypsin. Journal of the American Chemical Society, 94 (13). pp. 4573-4580. ISSN 0002-7863. http://resolver.caltech.edu/CaltechAUTHORS:20150429-133401521

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Abstract

Magnetic resonance studies of the interaction of N-trifluoroacetyl-n-(and L-)p-fluorophenylalanine with α-chymotrypsin have been used to investigate the molecular details of the enzyme-inhibitor interaction including the effect of pH (from 5.0 to 8.0). The principles of the technique are described. We conclude that the trifluoroacetyl group of then isomer interacts with the catalytic locus (His-57, Ser-195) while that of the L isomer is directed toward Ser-214. The aromatic ring of both then and L isomer resides in the hydrophobic pocket. The binding constant for the n isomer increases with neutralization of a group which has pK. of 6.6 in the free-enzyme (presumably His-57). The dimerization of chymotrypsin strongly affects the quantitative results and has been explicitly included in the analysis.


Item Type:Article
Related URLs:
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http://dx.doi.org/10.1021/ja00768a027DOIArticle
http://pubs.acs.org/doi/abs/10.1021/ja00768a027PublisherArticle
Additional Information:© 1972 American Chemical Society. Received October 6, 1971. This work was supported by a grant from the U. S. Public Health Service (GM-16424). One of us (K. L. G.) is also grateful for the support of an NSF Fellowship. The titrant was synthesized by R. B. Moon, who also carried out some early magnetic resonance studies on analogous systems. M. Hunkapiller and M. McMillan also contributed valuable synthetic assistance.
Funders:
Funding AgencyGrant Number
U. S. Public Health Service (USPHS)GM-16424
NSF FellowshipUNSPECIFIED
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Caltech Gates and Crellin Laboratories of Chemistry4319
Record Number:CaltechAUTHORS:20150429-133401521
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150429-133401521
Official Citation:Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to .alpha.-chymotrypsin Kenneth L. Gammon, Stephen H. Smallcombe, John H. Richards Journal of the American Chemical Society 1972 94 (13), 4573-4580 DOI: 10.1021/ja00768a027
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57093
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:01 May 2015 17:10
Last Modified:01 May 2015 17:10

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