An automated system for taking circular dichroism measurements of protein conformation has been developed by European scientists, freeing operator time and accelerating analysis.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
FEBS Lett. 2011 Apr 20;585(8):1197-202
Authors: Moehle K, Freund A, Kubli E, Robinson JA
The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a...
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08-02-2011 11:40 AM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
J Am Chem Soc. 2010 Dec 16;
Authors: Gossert AD, Hiller S, Ferna?ndez C
The detection and structural characterization of protein-ligand interactions by solution NMR is central to functional biology research as well as to drug discovery. Here we present a robust and highly automated procedure for obtaining the resonance assignments necessary for studies of such...
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12-18-2010 12:00 PM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Alvar D. Gossert, Sebastian Hiller and Ce?sar Ferna?ndez
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108383x/aop/images/medium/ja-2010-08383x_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108383x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/E3PMYeBSCeE
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12-17-2010 12:50 AM
[NMR paper] STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin
STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
Related Articles STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
J Biol Chem. 2005 Aug 12;280(32):29107-16
Authors: Megy S, Bertho G, Gharbi-Benarous J, Evrard-Todeschi N, Coadou G, Ségéral E, Iehle C, Quéméneur E, Benarous R, Girault JP
beta-TrCP is the F-box protein...
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11-25-2010 08:21 PM
[NMR paper] NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Related Articles NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Biochemistry. 2002 Feb 19;41(7):2149-57
Authors: Johnson MA, Rotondo A, Pinto BM
Transferred nuclear Overhauser enhancement (TRNOE) experiments have been performed at 800 MHz to investigate the bound conformation of the hexapeptide DRPVPY, a functional molecular mimic of the group A Streptococcus cell-wall polysaccharide. The hexapeptide binds to the monoclonal...
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11-24-2010 08:49 PM
[NMR paper] NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Related Articles NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Biochemistry. 1998 Jul 28;37(30):10616-25
Authors: Gizachew D, Moffett DB, Busse SC, Westler WM, Dratz EA, Teintze M
A peptide containing residues 36-59 of the human CD4 receptor includes most of the residues thought to be involved in binding the HIV surface glycoprotein, gp120. This peptide was synthesized and inhibited the binding of gp120 to soluble CD4. NMR relaxation...
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11-17-2010 11:15 PM
[NMR paper] NMR and CD studies on the conformation of a synthetic peptide containing epitopes of
NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Related Articles NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Biopolymers. 1996 Mar;38(3):423-35
Authors: Consonni R, Limiroli R, Longhi R, Manera E, Vecchio G, Ragona L, Siccardi AG, Zetta L
CD and nmr characterizations are reported for the 23-mer peptide CMC3, corresponding to residues 577-599...
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08-22-2010 02:27 PM
[NMR paper] NMR studies of retinoid-protein interactions: the conformation of [13C]-beta-ionones
NMR studies of retinoid-protein interactions: the conformation of -beta-ionones bound to beta-lactoglobulin B.
Related Articles NMR studies of retinoid-protein interactions: the conformation of -beta-ionones bound to beta-lactoglobulin B.
Pharm Res. 1999 May;16(5):651-9
Authors: Curley RW, Sundaram AK, Fowble JW, Abildgaard F, Westler WM, Markley JL
PURPOSE: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic...
Automated protein conformation studies
An automated system for taking circular dichroism measurements of protein conformation has been developed by European scientists, freeing operator time and accelerating analysis.
Linear Mode
