rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2003-3-11
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0006-2960
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
18
|
pubmed:volume |
42
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
2774-80
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12627942-Binding Sites,
pubmed-meshheading:12627942-Calcium-Binding Proteins,
pubmed-meshheading:12627942-Carrier Proteins,
pubmed-meshheading:12627942-Membrane Glycoproteins,
pubmed-meshheading:12627942-Mitochondrial Proteins,
pubmed-meshheading:12627942-Nerve Tissue Proteins,
pubmed-meshheading:12627942-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12627942-Protein Binding,
pubmed-meshheading:12627942-Protein Interaction Mapping,
pubmed-meshheading:12627942-Protein Structure, Tertiary,
pubmed-meshheading:12627942-Proteins,
pubmed-meshheading:12627942-Solutions,
pubmed-meshheading:12627942-Synaptotagmin I,
pubmed-meshheading:12627942-Synaptotagmins,
pubmed-meshheading:12627942-X-Linked Inhibitor of Apoptosis Protein
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pubmed:year |
2003
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pubmed:articleTitle |
Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
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pubmed:affiliation |
Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9038, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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