[NMR paper] Validation of the binding site structure of the cellular retinol-binding protein (CRB
Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations.
Related Articles Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations.
J Am Chem Soc. 2005 Apr 20;127(15):5310-1
Authors: Wang B, Merz KM
We have calculated proton chemical shift perturbations (CSPs) of retinol in the cellular retinol-binding protein (CRBP) through the use of a recently developed computational approach (Wang et al. J....
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11-25-2010 08:21 PM
[NMR paper] NMR structure and peptide hormone binding site of the first extracellular domain of a
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Related Articles NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41
Authors: Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands'...
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11-24-2010 10:01 PM
[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] Proton NMR investigation of the heme active site structure of an engineered cytochrom
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Related Articles Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Biochemistry. 1999 Jul 13;38(28):9146-57
Authors: Wang X, Lu Y
The heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensional NMR spectroscopy. All...
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11-18-2010 08:31 PM
[NMR paper] NMR studies of the most conserved RNA domain of the mammalian signal recognition part
NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP).
RNA. 1996 Dec;2(12):1213-27
Authors: Schmitz U, Freymann DM, James TL, Keenan RJ, Vinayak R, Walter P
Mammalian signal recognition particle (SRP) and its homologues exhibit a phylogenetically conserved RNA domain, whose...
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08-22-2010 02:20 PM
[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...
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08-22-2010 03:29 AM
[NMR paper] Solution conformation of a peptide fragment representing a proposed RNA-binding site
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR.
Related Articles Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR.
Biochemistry. 1991 Jun 11;30(23):5722-7
Authors: van der Graaf M, van Mierlo CP, Hemminga MA
The first 25 amino acids of the coat protein of cowpea chlorotic mottle virus are essential for binding the encapsidated RNA. Although an alpha-helical...
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08-21-2010 11:16 PM
[NMR paper] Direct measurement of agonist binding to genetically engineered peptides of the acety
Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Related Articles Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Biochemistry. 1990 Mar 13;29(10):2617-22
Authors: Fraenkel Y, Navon G, Aronheim A, Gershoni JM
Interactions of four ligands of the nicotinic acetylcholine receptor with genetically engineered peptides have been studied by NMR. A recombinant cholinergic binding...
Conserved SecA Signal Peptide-Binding Site Revealedby Engineered Protein Chimeras and Fo?rster Resonance EnergyTransfer
Linear Mode
