Related ArticlesA structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.
J Mol Biol. 1998;283(1):205-19
Authors: Boisbouvier J, Albrand JP, Blackledge M, Jaquinod M, Schweitz H, Lazdunski M, Marion D
The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution.
Triple resonance three-dimensional protein NMR: Before it became a black box.
Triple resonance three-dimensional protein NMR: Before it became a black box.
Triple resonance three-dimensional protein NMR: Before it became a black box.
J Magn Reson. 2011 Aug 30;
Authors: Bax A
Abstract
Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with (13)C and (15)N, and establishes the scalar connectivity pathway between nuclei through the large (1)J(NH), (1)J(CH)(, 1)J(CC), and (1)J(CN)...
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Triple resonance three-dimensional protein NMR: Before it became a black box
Triple resonance three-dimensional protein NMR: Before it became a black box
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 31 August 2011</br>
Ad, Bax</br>
Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with 13C and 15N, and establishes the scalar connectivity pathway between nuclei through the large 1JNH, 1JCH, 1JCC, and 1JCN couplings. The magnetization transfer process takes place...
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08-31-2011 07:12 PM
[Ryan's blog] The Black Swan of Compound Libraries
Source: Ryan's blog
The Black Swan of Compound Libraries
Recently I finished a great book that made me think about different things on a lot of different levels. The book is called The Black Swan and the author is Nassim Nicholas Taleb. In short, a black swan is defined...
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02-21-2011 10:57 PM
[NMR paper] Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis,
Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches.
Related Articles Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches.
Structure. 2004 Apr;12(4):633-44
Authors: Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R
The protein CNOT4 possesses an N-terminal RING finger domain that acts as an E3 ubiquitin ligase and specifically interacts with UbcH5B, a ubiquitin-conjugating enzyme. The structure of the CNOT4...
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11-24-2010 09:51 PM
[NMR paper] NMR structure of an archaeal homologue of ribonuclease P protein Rpp29.
NMR structure of an archaeal homologue of ribonuclease P protein Rpp29.
Related Articles NMR structure of an archaeal homologue of ribonuclease P protein Rpp29.
Biochemistry. 2003 Nov 25;42(46):13541-50
Authors: Sidote DJ, Hoffman DW
A protein component of the Archaeoglobus fulgidus RNase P was expressed in Escherichia coli, purified, and structurally characterized using multidimensional NMR methods. The dominant structural feature of this 11 kDa protein is a sheet of six antiparallel beta-strands, wrapped around a core of conserved...
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[NMR paper] Structural preordering in the N-terminal region of ribosomal protein S4 revealed by h
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy.
Related Articles Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy.
Biochemistry. 2000 Nov 7;39(44):13602-13
Authors: Sayers EW, Gerstner RB, Draper DE, Torchia DA
Protein S4, a component of the 30S subunit of the prokaryotic ribosome, is one of the first proteins to interact with rRNA in the process of ribosome assembly and is known to be involved in the regulation...
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11-19-2010 08:29 PM
[NMR paper] Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Related Articles Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Biochemistry. 1991 Dec 17;30(50):11625-36
Authors: Chen Y, Pitzenberger SM, Garsky VM, Lumma PK, Sanyal G, Baum J
The snake venom protein echistatin is a potent inhibitor of platelet aggregation. The inhibitory properties of echistatin have been attributed to the Arg-Gly-Asp sequence at residues 24-26. In this paper, sequence-specific nuclear magnetic...
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[NMR paper] Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Related Articles Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Biochemistry. 1991 Dec 17;30(50):11625-36
Authors: Chen Y, Pitzenberger SM, Garsky VM, Lumma PK, Sanyal G, Baum J
The snake venom protein echistatin is a potent inhibitor of platelet aggregation. The inhibitory properties of echistatin have been attributed to the Arg-Gly-Asp sequence at residues 24-26. In this paper, sequence-specific nuclear magnetic...
A structural homologue of colipase in black mamba venom revealed by NMR floating disu
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