[NMR paper] Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Related Articles Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Anal Chem. 2013 May 22;
Authors: Maple HJ, Garlish RA, Whitcombe I, Hold A, Prosser CE, Ford D, Mackenzie H, Crosby J, Porter J, Taylor RJ, Crump MP
Abstract
Atropisomerism of...
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05-24-2013 10:44 PM
Identification of Cryptic Products of the Gliotoxin Gene Cluster Using NMR-Based Comparative Metabolomics and a Model for Gliotoxin Biosynthesis
Identification of Cryptic Products of the Gliotoxin Gene Cluster Using NMR-Based Comparative Metabolomics and a Model for Gliotoxin Biosynthesis
Ry R. Forseth, Ellen M. Fox, DaWoon Chung, Barbara J. Howlett, Nancy P. Keller and Frank C. Schroeder
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2029987/aop/images/medium/ja-2011-029987_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2029987
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/kET0fe1YTXQ
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06-07-2011 01:01 AM
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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[NMR paper] Calbindin D28K interacts with Ran-binding protein M: identification of interacting do
Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Related Articles Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92
Authors: Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R
Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts...
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11-24-2010 09:01 PM
[NMR paper] In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5
In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
Related Articles In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
J Med Chem. 2002 Dec 19;45(26):5655-60
Authors: Kamionka M, Rehm T, Beisel HG, Lang K, Engh RA, Holak TA
Recently we have determined the crystal structure of the insulin-like growth factor-I (IGF-I) in complex with the N-terminal domain of the IGF-binding protein-5 (IGFBP-5). Here we report results of computer screening for...
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[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
...
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11-19-2010 08:29 PM
[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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11-18-2010 08:31 PM
[NMR paper] Identification of reaction products and intermediates of aromatic-amine dehydrogenase
Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR.
Related Articles Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR.
Biochem J. 1998 Mar 15;330 ( Pt 3):1159-63
Authors: Bishop GR, Zhu Z, Whitehead TL, Hicks RP, Davidson VL
13C- and 15N-NMR studies of the reaction of aromatic amine dehydrogenase (AADH) with methylamine demonstrated that the products of the reductive half-reaction are an equivalent of formaldehyde hydrate and a reduced...
Identification of C1q as a Binding Protein for AdvancedGlycation End Products
Linear Mode
