NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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07-30-2011 11:23 AM
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
J Biol Chem. 2011 Jan 26;
Authors: Lemke CT, Goudreau N, Zhao S, Hucke O, Thibeault D, Llinás-Brunet M, White PW
Hepatitis C virus (HCV) infection, a major cause of liver disease world-wide, is curable but currently approved therapies have suboptimal efficacy. Supplementing these therapies...
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01-29-2011 12:35 PM
[NMR paper] NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal u
NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability.
Related Articles NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability.
J Mol Biol. 2002 Aug 23;321(4):647-58
Authors: Cierpicki T, Otlewski J
Here we determined NMR solution structures of two mutants of bovine pancreatic trypsin inhibitor (BPTI) to reveal structural reasons of their decreased...
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11-24-2010 08:58 PM
[NMR paper] NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: cha
NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
Related Articles NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
J Mol Recognit. 2001 May-Jun;14(3):166-71
Authors: Song J, Markley JL
The substrate-like...
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11-19-2010 08:32 PM
[NMR paper] The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex
The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
Related Articles The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
J Mol Biol. 1999 Sep 3;291(5):1067-77
Authors: Wilkinson KD, Laleli-Sahin E, Urbauer J, Larsen CN, Shih GH, Haas AL, Walsh ST, Wand AJ
The ubiquitin fold is a versatile and widely used targeting signal that is added post-translationally to a variety of proteins. Covalent attachment of one or more...
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11-18-2010 08:31 PM
[NMR paper] NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
Related Articles NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
Protein Sci. 1999 Aug;8(8):1711-3
Authors: Hannan JP, Whittaker SB, Davy SL, Kühlmann UC, Pommer AJ, Hemmings AM, James R, Kleanthous C, Moore GR
Ni2+ affinity columns are widely used for protein purification, but they carry the risk that Ni2+ ions may bind to the protein, either adventitiously or at a physiologically important site. Dialysis against ethylenediaminetetraacetic acid...
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11-18-2010 08:31 PM
[NMR paper] The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii
The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Related Articles The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Eur J Biochem. 1998 Jul 1;255(1):185-95
Authors: Krimm I, Lemaire S, Ruelland E, Miginiac-Maslow M, Jaquot JP, Hirasawa M, Knaff DB, Lancelin JM
The role of the invariant Trp...
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11-17-2010 11:15 PM
[NMR paper] pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thi
pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR.
Related Articles pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR.
J Biol Chem. 1990 Feb 15;265(5):2768-74
Authors: Lommen A, Canters GW
The kinetics of the deuteronation of one of the copper ligand histidines of the reduced Type I blue-copper protein amicyanin from Thiobacillus versutus was studied as a...
NMR Studies Reveal anUnexpected Binding Site for a Redox Inhibitor of AP Endonuclease 1
Linear Mode
