Related ArticlesNMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a recombinant cholinergic binding site (T alpha 184-200 expressed as a fusion protein in Escherichia coli). The conformations of the free ligands were determined by NOESY experiments while those of the bound molecules were obtained by transferred NOESY. The complete relaxation matrix was solved yielding distance constraints which were further refined by a sigma back-calculation. ACh bound to recombinant T alpha 184-200 closely resembled the conformation previously reported for ACh bound to the intact receptor. d-Tubocurarine in the bound state undergoes extensive induced conformational rearrangements generating a "cup"-shaped structure. A unique positively charged hydrophobic domain is identified as characteristic of both bound cholinergic ligands.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....
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12-15-2010 12:03 PM
NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin,
NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin,
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101594a/aop/images/medium/bi-2010-01594a_0006.gif
Biochemistry
DOI: 10.1021/bi101594a
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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12-15-2010 12:16 AM
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Related Articles NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Biochemistry. 2010 Dec 1;
Authors: Lange A, Hoeller D, Wienk H, Marcillat O, Lancelin JM, Walker O
The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation. Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to...
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12-03-2010 08:52 PM
[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
J Magn Reson. 2005 Jul;175(1):158-62
Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ
Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...
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11-25-2010 08:21 PM
[NMR paper] NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking t
NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
Related Articles NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
J Mol Biol. 2001 Sep 7;312(1):167-75
Authors: Hanaoka S, Nagadoi A, Yoshimura S, Aimoto S, Li B, de Lange T, Nishimura Y
Mammalian telomeres are composed of long tandem arrays of double-stranded telomeric TTAGGG repeats associated with...
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11-19-2010 08:44 PM
[NMR paper] NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide
NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide.
Related Articles NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide.
Biochim Biophys Acta. 1998 Nov 8;1442(2-3):137-47
Authors: van Lieshout E, Hemminga MA
To obtain a better understanding of the electrostatic nature of protein-nucleic acid interactions, we have investigated the interaction of a double-stranded decamer d(GGAAATTTCC)2 with a synthetic arginine and lysine-rich pentacosapeptide (Pep25), using NMR and optical...
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11-17-2010 11:15 PM
[NMR paper] NMR structure and dynamics of an RNA motif common to the spliceosome branch-point hel
NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Related Articles NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Biochemistry. 1998 Sep 29;37(39):13486-98
Authors: Smith JS, Nikonowicz EP
The RNA molecules that make up the spliceosome branch-point helix and the binding site for phage GA coat protein share a secondary structure motif in which two consecutive...
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11-17-2010 11:15 PM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
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