Related ArticlesFacile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
Biochemistry. 2003 Mar 18;42(10):2774-80
Authors: Araç D, Murphy T, Rizo J
Two methods for detecting protein-protein interactions in solution using one-dimensional (1D) NMR spectroscopy are described. Both methods rely on measurement of the intensity of the strongest methyl resonance (SMR), which for most proteins is observed at 0.8-0.9 ppm. The severe resonance overlap in this region facilitates detection of the SMR at low micromolar and even sub-micromolar protein concentrations. A decreased SMR intensity in the 1H NMR spectrum of a protein mixture compared to the added SMR intensities of the isolated proteins reports that the proteins interact (SMR method). Decreased SMR intensities in 1D 13C-edited 1H NMR spectra of 13C-labeled proteins upon addition of unlabeled proteins or macromolecules also demonstrate binding (SMRC method). Analysis of the interaction between XIAP and Smac, two proteins involved in apoptosis, illustrates both methods. A study showing that phospholipids compete with the neuronal core complex for Ca2+-dependent binding to the presynaptic Ca2+-sensor synaptotagmin 1 illustrates the usefulness of the SMRC method in studying multicomponent systems.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
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Journal club
0
09-30-2011 05:59 AM
[NMR paper] Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy.
Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy.
Related Articles Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13220-6
Authors: D'Silva L, Ozdowy P, Krajewski M, Rothweiler U, Singh M, Holak TA
We describe an NMR method that directly monitors the influence of ligands on protein-protein interactions. For a two-protein interaction complex, the size of one component should be small enough (less than ca. 15 kDa) to provide...
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12-01-2010 06:56 PM
[NMR paper] New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Related Articles New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Curr Opin Struct Biol. 2003 Oct;13(5):646-53
Authors: Kogelberg H, Solís D, Jiménez-Barbero J
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the...
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11-24-2010 09:16 PM
[NMR paper] Detection of the protein-protein interaction between cyclic AMP receptor protein and
Detection of the protein-protein interaction between cyclic AMP receptor protein and RNA polymerase, by (13)C-carbonyl NMR.
Related Articles Detection of the protein-protein interaction between cyclic AMP receptor protein and RNA polymerase, by (13)C-carbonyl NMR.
J Biochem. 2001 Jul;130(1):57-61
Authors: Lee TW, Won HS, Park SH, Kyogoku Y, Lee BJ
Cyclic AMP receptor protein (CRP) plays a key role in the transcription regulation of many prokaryotic genes. Upon the binding of cyclic AMP, CRP is allosterically activated, binds to target DNA...
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11-19-2010 08:44 PM
[NMR paper] NMR investigations of protein-carbohydrate interactions: refined three-dimensional st
NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside.
Related Articles NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside.
Glycobiology. 1998 Jun;8(6):569-77
Authors: Asensio JL, Cañada FJ, Bruix M, González C, Khiar N, Rodríguez-Romero A, Jiménez-Barbero J
The specific interaction of hevein with GlcNAc-containing oligosaccharides has been...
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11-17-2010 11:06 PM
Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low c
Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low concentration of protein.
Related Articles Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low concentration of protein.
Magn Reson Chem. 2010 Oct 18;
Authors: Xia Y, Zhu Q, Jun KY, Wang J, Gao X
Saturation transfer difference (STD)-NMR has been widely used to screen ligand compound libraries for their binding activities to proteins and to determine the binding epitopes of the ligands. We report herein, a Clean STD-NMR method...
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10-22-2010 06:02 AM
[NMR paper] Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: th
Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
Related Articles Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
J Biomol NMR. 1993 May;3(3):285-96
Authors: Stockman BJ, Euvrard A, Scahill TA
Human ubiquitin is a 76-residue protein that serves as a protein degradation signal when conjugated to another protein. Ubiquitin has been shown to exist in at least three states: native (N-state), unfolded (U-state), and,...
Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
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