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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0014406,
umls-concept:C0025965,
umls-concept:C0031694,
umls-concept:C0041249,
umls-concept:C0243071,
umls-concept:C0439097,
umls-concept:C0442726,
umls-concept:C0596988,
umls-concept:C0917874,
umls-concept:C1511790,
umls-concept:C1547348,
umls-concept:C1705241,
umls-concept:C1708096,
umls-concept:C1880022
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pubmed:issue |
25
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pubmed:dateCreated |
1998-7-20
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pubmed:abstractText |
Phosphorescence and optically detected magnetic resonance (ODMR) measurements are reported on the triplet states of the tryptophan analogues, 7-azatryptophan (7AW), 5-hydroxytryptophan (5HW), and 4-, 5-, and 6-fluorotryptophan (4FW, 5FW, 6FW), when incorporated at position 140 of wild-type Staphylococcal nuclease (7AW-nuclease, etc. ), positions 66 and 140 of its V66W mutant (7AW-V66W, etc.), and the deletion fragment of the latter, Delta 137-149 (7AW-V66W', etc.). These measurements point to the retention of protein structure at position 140 in each of the wild-type nuclease analogues. Substitution of the analogue at both tryptophan sites of V66W leads to structured sites with differentiated triplet-state properties for all analogues except 7AW-V66W, whose structure is destabilized. 5HW-V66W' is the only fragment that apparently lacks structure at position 66. All other V66W' analogues exhibit a structured environment at position 66 (4FW-V66W' was not studied), but in each case this site can be differentiated readily from the corresponding site in intact V66W. 7AW-V66W' is resolved by ODMR into two discrete structures with slightly differing zero field splittings (ZFS). Interaction of the protein with 5HW at position 66 of 5HW-V66W induces a 2-fold increase in the ZFS E parameter, which is reduced to its normal value upon formation of the fragment, 5HW-V66W'. Analogous effects occur for 5FW, but on a smaller scale.
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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/4-fluorotryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/5-Hydroxytryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/5-fluorotryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/6-fluorotryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/7-azatryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Micrococcal Nuclease,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8954-64
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9636037-5-Hydroxytryptophan,
pubmed-meshheading:9636037-Amino Acid Substitution,
pubmed-meshheading:9636037-Luminescent Measurements,
pubmed-meshheading:9636037-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9636037-Micrococcal Nuclease,
pubmed-meshheading:9636037-Mutagenesis, Site-Directed,
pubmed-meshheading:9636037-Peptide Fragments,
pubmed-meshheading:9636037-Tryptophan,
pubmed-meshheading:9636037-Valine
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pubmed:year |
1998
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pubmed:articleTitle |
Phosphorescence and optically detected magnetic resonance characterization of the environments of tryptophan analogues in staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment.
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pubmed:affiliation |
Department of Chemistry, University of California, Davis 95616, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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