Literature DB >> 7530321

Nuclear magnetic resonance methods for studying protein-ligand complexes.

A M Petros1, S W Fesik.   

Abstract

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Year:  1994        PMID: 7530321     DOI: 10.1016/s0076-6879(94)39027-4

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


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  4 in total

1.  NMR-restrained docking of a peptidic inhibitor to the N-terminal domain of the phosphoenolpyruvate:sugar phosphotransferase enzyme I.

Authors:  D Rognan; S Mukhija; G Folkers; O Zerbe
Journal:  J Comput Aided Mol Des       Date:  2001-02       Impact factor: 3.686

Review 2.  The other kind of biological NMR--studies of enzyme-substrate interactions.

Authors:  G C Roberts
Journal:  Neurochem Res       Date:  1996-09       Impact factor: 3.996

3.  Physicochemical consequences of the perdeuteriation of glutathione S-transferase from S. japonicum.

Authors:  D Brockwell; L Yu; S Cooper; S McCleland; A Cooper; D Attwood; S J Gaskell; J Barber
Journal:  Protein Sci       Date:  2001-03       Impact factor: 6.725

Review 4.  On the Rational Drug Design for Hypertension through NMR Spectroscopy.

Authors:  Eleni Chontzopoulou; Andreas G Tzakos; Thomas Mavromoustakos
Journal:  Molecules       Date:  2020-12-22       Impact factor: 4.411

  4 in total

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