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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7-8
|
| pubmed:dateCreated |
1986-2-28
|
| pubmed:abstractText |
A procedure is described to determine from NMR data the three-dimensional structure of biomolecules. This procedure combines model building with a restrained Molecular Dynamics algorithm, in which distance information from NOEs is incorporated in the form of pseudo potentials. The method has been applied to the N-terminal DNA-binding domain or "headpiece" (amino acids 1-51) of the lac repressor from E. coli, for which no crystal structure is available. The spatial structure of the headpiece is discussed in terms of known physical and biochemical data and of its DNA binding properties.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
67
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
707-15
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:3910108-Binding Sites,
pubmed-meshheading:3910108-DNA,
pubmed-meshheading:3910108-Escherichia coli,
pubmed-meshheading:3910108-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3910108-Models, Molecular,
pubmed-meshheading:3910108-Nucleic Acid Conformation,
pubmed-meshheading:3910108-Protein Binding,
pubmed-meshheading:3910108-Protein Conformation,
pubmed-meshheading:3910108-Repressor Proteins,
pubmed-meshheading:3910108-Transcription Factors
|
| pubmed:articleTitle |
Determination of protein structures from nuclear magnetic resonance data using a restrained molecular dynamics approach: the lac repressor DNA binding domain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|