Raftery, M. A. and Dahlquist, F. W. and Parsons, S. M. and Wolcott, R. G. (1969) The use of nuclear magnetic resonance to describe relative modes of binding to lysozyme of homologous inhibitors and related substrates. Proceedings of the National Academy of Sciences of the United States of America, 62 (1). pp. 44-51. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:RAFpnas69
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Proton magnetic resonance has been used to study the association of inhibitors and substrates with hen egg-white lysozyme. Changes in chemical shift, due to association, of acetamido methyl group resonances of the small molecules have been quantitated. This has allowed definition of magnetic parameters for three contiguous binding subsites on the enzyme surface. The relative modes of occupancy of these sites by N-acetyl-D-glucosamine (NAG), chitobiose, chitotriose, their methyl glycosides, and chitotetraose have been delineated. In addition, the binding to these sites of N-acetyl-D-muramic acid (NAM) and a cell-wall disaccharide, NAG-NAM, have been studied. There is good, although not complete, agreement between the results obtained and X-ray analysis studies of the binding of some of these inhibitors to crystalline lysozyme. Binding of synthetic substrates, such as p-nitrophenyl-2-acetamido-4-O-(2-acetamido-2-deoxy-ß -D-glucopyranosyl)-ß -D-glucopyranoside (NAG-Gluc- ΦNO2), has also been studied by the magnetic resonance technique described.
|Additional Information:||© 1969 by the National Academy of Sciences. Communicated by John D. Roberts, September 9, 1968. This research was supported by grant no. GM-14452 of the U.S. Public Health Service. A preliminary account of portions of this work was given at the Gordon Research Conference on Proteins, New Hampton, June 2, 1966. [F.W.D., S.M.P., and R.G.W. were] U.S. Public Health Service Trainees. Gates and Crellin Laboratories of Chemistry, Contribution No. 3745.|
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|Deposited By:||Tony Diaz|
|Deposited On:||28 Feb 2007|
|Last Modified:||26 Dec 2012 09:32|
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