Literature DB >> 16895

31P nuclear magnetic resonance of bound substrates of arginine kinase reaction: chemical shifts in binary, ternary, quaternary, and transition state analog complexes.

B D Rao, M Cohn.   

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Year:  1977        PMID： 16895

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  5 in total

1.  Asymmetric binding of the inhibitor di(adenosine-5') pentaphosphate (Ap5A) to adenylate kinase.

Authors:  B D Nageswara Rao; M Cohn
Journal:  Proc Natl Acad Sci U S A       Date:  1977-12       Impact factor: 11.205

2.  The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.

Authors:  Yu Peng; Alexandar L Hansen; Lei Bruschweiler-Li; Omar Davulcu; Jack J Skalicky; Michael S Chapman; Rafael Brüschweiler
Journal:  J Am Chem Soc       Date:  2017-03-27       Impact factor: 15.419

3.  Phosphorus nuclear-magnetic-resonance studies of the transition-state analogue complex of creatine kinase.

Authors:  E J Milner-White; D S Rycroft
Journal:  Biochem J       Date:  1977-12-01       Impact factor: 3.857

4.  Rate-limiting domain and loop motions in arginine kinase.

Authors:  Omar Davulcu; Jack J Skalicky; Michael S Chapman
Journal:  Biochemistry       Date:  2011-04-22       Impact factor: 3.162

5.  Compartmentation of Nucleotides in Corn Root Tips Studied by P-NMR and HPLC.

Authors:  M A Hooks; R A Clark; R H Nieman; J K Roberts
Journal:  Plant Physiol       Date:  1989-03       Impact factor: 8.340
  5 in total

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