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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1994-4-25
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pubmed:abstractText |
Solid-state deuterium NMR spectroscopy is used to examine the dynamic behavior of 18-CD3 methyl groups in microcrystalline 6-s-cis-retinoic acid (triclinic) and 6-s-trans-retinoic acid (monoclinic) model compounds, as well as in the membrane protein bacteriorhodopsin (bR), regenerated with CD3-labeled retinal. Temperature dependent quadrupolar echo line shapes and T1 anisotropy measurements were used to characterize activation energies for 3-fold hopping motion of the methyl groups. These data provide supporting evidence that the conformation of the retinal chromophore in bR is 6-s-trans. The 6-s-cis conformer is characterized by strong eclipsing interactions between the 8-C proton and the 18-C methyl group protons; the 18-CD3 group shows an activation energy barrier for methyl 3-fold hopping of 14.5 +/- 1 kJ/mol. In contrast, the 18-CD3 group in the 6-s-trans isomer shows a considerably lower activation energy barrier of 5 +/- 1 kJ/mol. In bR, it is possible to obtain an approximate activation energy of 9 kJ/mol. This data is inconsistent with a 6-s-cis conformer but is consistent with the existence of a 6-s-trans-retinal Schiff base in bR with some interaction with the protein matrix. These results suggest that methyl rotor motions can be used to probe the van der Waals contact between a ligand and a protein binding pocket. The 6-s-trans conformer of the [16,17-(CD3)2]retinal in frozen hexane exhibits a major kinetic component with an activation energy barrier of of 14 -/+ 2 kJ/mol.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacteriorhodopsins,
http://linkedlifedata.com/resource/pubmed/chemical/Deuterium,
http://linkedlifedata.com/resource/pubmed/chemical/Hexanes,
http://linkedlifedata.com/resource/pubmed/chemical/Retinaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3280-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8136363-Bacteriorhodopsins,
pubmed-meshheading:8136363-Chemistry, Physical,
pubmed-meshheading:8136363-Computer Simulation,
pubmed-meshheading:8136363-Crystallization,
pubmed-meshheading:8136363-Deuterium,
pubmed-meshheading:8136363-Freezing,
pubmed-meshheading:8136363-Hexanes,
pubmed-meshheading:8136363-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8136363-Physicochemical Phenomena,
pubmed-meshheading:8136363-Protein Conformation,
pubmed-meshheading:8136363-Retinaldehyde,
pubmed-meshheading:8136363-Temperature,
pubmed-meshheading:8136363-Thermodynamics,
pubmed-meshheading:8136363-Tretinoin
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pubmed:year |
1994
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pubmed:articleTitle |
Deuterium solid-state nuclear magnetic resonance studies of methyl group dynamics in bacteriorhodopsin and retinal model compounds: evidence for a 6-s-trans chromophore in the protein.
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pubmed:affiliation |
Francis Bitter National Magnet Laboratory, Massachusetts Institute of Technology, Cambridge 02139.
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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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