rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
19
|
pubmed:dateCreated |
1983-10-28
|
pubmed:abstractText |
A recently proposed approach for spatial structure determination in noncrystalline proteins by nuclear magnetic resonance was applied to the lac repressor DNA-binding domain. On the basis of sequence-specific 1H NMR assignments, the location of alpha-helices in the amino acid sequence was determined from nuclear Overhauser enhancement data and from amide proton exchange studies. These investigations provide detailed experimental data on the structure of a noncrystalline DNA-binding protein. The results support the hypothesis advanced by others that sequence-specific interactions between lac repressor and DNA are mediated by a particular spatial arrangement of two alpha-helices common to various different DNA-binding proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-231106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-321012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-365582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-372550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-385890,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/6351066-779429
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0027-8424
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
80
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5837-41
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
|
pubmed:year |
1983
|
pubmed:articleTitle |
Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|