Literature DB >> 6074810

Enzyme--substrate interaction by nuclear magnetic resonance.

T Spotswood, J M Evans, J H Richards.   

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Year:  1967        PMID： 6074810     DOI： 10.1021/ja00995a047

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


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  4 in total

Review 1.  Use of 19F NMR to probe protein structure and conformational changes.

Authors:  M A Danielson; J J Falke
Journal:  Annu Rev Biophys Biomol Struct       Date:  1996

2.  13C high-resolution nuclear magnetic resonance studies of enzyme-substrate reactions at equilibrium. Substrate studies of chymotrypsin-N-acetyltyrosine semicarbazide complexes.

Authors:  G Robillard; E Shaw; R G Shulman
Journal:  Proc Natl Acad Sci U S A       Date:  1974-07       Impact factor: 11.205

3.  Conformations of diphosphopyridine coenzymes upon binding to dehydrogenases.

Authors:  C Y Lee; R D Eichner; N O Kaplan
Journal:  Proc Natl Acad Sci U S A       Date:  1973-05       Impact factor: 11.205

4.  The use of nuclear magnetic resonance to describe relative modes of binding to lysozyme of homologous inhibitors and related substrates.

Authors:  M A Raftery; F W Dahlquist; S M Parsons; R G Wolcott
Journal:  Proc Natl Acad Sci U S A       Date:  1969-01       Impact factor: 11.205
  4 in total

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