Source:http://linkedlifedata.com/resource/pubmed/id/15939999
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2005-6-7
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pubmed:abstractText |
Interaction between biological macromolecules or of macromolecules with low-molecular-weight ligands is a central paradigm in the understanding of function in biological systems. It is also the major goal in pharmaceutical research to find and optimize ligands that modulate the function of biological macromolecules. Both technological advances and new methods in the field of nuclear magnetic resonance (NMR) have led to the development of several tools by which the interaction of proteins or DNA and low molecular weight-ligands can be characterized at an atomic level. Information can be gained quickly and easily with ligand-based techniques. These need only small amounts of nonisotope labeled, and thus readily available target macromolecules. As the focus is on the signals stemming only from the ligand, no further NMR information regarding the target is needed. Techniques based on the observation of isotopically labeled biological macromolecules open the possibility to observe interactions of proteins with low-molecular-weight ligands, DNA or other proteins. With these techniques, the structure of high-molecular-weight complexes can be determined. Here, the resonance signals of the macromolecule must be identified beforehand, which can be time consuming but with the benefit of obtaining more information with respect to the target ligand complex.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin
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pubmed:status |
MEDLINE
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pubmed:issn |
1064-3745
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
305
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
197-214
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pubmed:dateRevised |
2009-11-3
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pubmed:meshHeading |
pubmed-meshheading:15939999-Binding Sites,
pubmed-meshheading:15939999-Carbon Isotopes,
pubmed-meshheading:15939999-Humans,
pubmed-meshheading:15939999-Ligands,
pubmed-meshheading:15939999-Macrophages,
pubmed-meshheading:15939999-Models, Molecular,
pubmed-meshheading:15939999-Nitrogen Isotopes,
pubmed-meshheading:15939999-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:15939999-Pancreatic Elastase,
pubmed-meshheading:15939999-Protein Binding,
pubmed-meshheading:15939999-Proteins,
pubmed-meshheading:15939999-Serum Albumin
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pubmed:year |
2005
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pubmed:articleTitle |
NMR studies of protein-ligand interactions.
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pubmed:affiliation |
Department of Lead Discovery, Boehringer Ingelheim Pharma GmbH & Co. KG, Biberach, Germany.
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pubmed:publicationType |
Journal Article,
In Vitro
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