Literature DB >> 5781005

A transient nuclear magnetic resonance study of the kinetics of methyl N-acetyl-D-glucosaminide inhibition of lysozyme.

B D Sykes.   

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Year:  1969        PMID： 5781005     DOI： 10.1021/bi00831a043

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Stopped-flow fluorescence studies on saccharide binding to lysozyme.

Authors:  S E Halford
Journal:  Biochem J       Date:  1975-08       Impact factor: 3.857

2.  The interaction of N-trifluoroacetylgalactosamine and its derivatives with winged bean (Psophocarpus tetragonolobus) basic agglutinin reveals differential mechanism of their recognition: a fluorine-19 nuclear magnetic resonance study.

Authors:  Samiksha Katiyar; Amrita Singh; Avadhesha Surolia
Journal:  Glycoconj J       Date:  2014-10       Impact factor: 2.916

3.  Crystal structures of egg-white lysozyme of hen in acetate-free medium and of lysozyme complexes with N-acetylglucosamine and beta-methyl N-acetylglucosaminide.

Authors:  S J Perkins; L N Johnson; P A Machin; D C Phillips
Journal:  Biochem J       Date:  1978-08-01       Impact factor: 3.857

4.  The binding of monosaccharide inhibitors to hen egg-white lysozyme by proton magnetic resonance at 270 MHz and analysis by ring-current calculations.

Authors:  S J Perkins; L N Johnson; D C Phillips; R A Dwek
Journal:  Biochem J       Date:  1981-02-01       Impact factor: 3.857

5.  The simultaneous binding of lanthanide and N-acetylglucosamine inhibitors to hen egg-white lysozyme in solution by 1H and 13C nuclear magnetic resonance.

Authors:  S J Perkins; L N Johnson; D C Phillips; R A Dwek
Journal:  Biochem J       Date:  1981-02-01       Impact factor: 3.857
  5 in total

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