Source:http://linkedlifedata.com/resource/pubmed/id/17555338
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
2007-6-26
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pubmed:abstractText |
In this paper, we studied the surface properties of recombinant aequorin at the air-water interface. Using the Langmuir monolayer technique, the surface properties of aequorin were studied, including the surface pressure and surface potential-area isotherms, compression-decompression cycles, and stability on Trizma Base (Tris/HCl) buffer at pH 7.6. The results showed that aequorin formed a stable Langmuir monolayer and the surface pressure-area isotherms were dependent on both pH and ionic strength. At a pH higher or lower than 7.6, the limiting molecular area decreased. The circular dichroism (CD) spectra of aequorin in aqueous solutions explained this result: when the pH was higher than 7.6, the alpha-helix conformation changed to unordered structures, whereas at a pH lower than 7.6, the alpha-helix conformation changed to beta-sheet. The addition of calcium chloride to the Tris/HCl buffer subphase (pH 7.6) caused an increase of the limiting molecular area of the aequorin Langmuir monolayer. The fluorescence spectra of a Langmuir-Blodgett (LB) film of aequorin in the presence of calcium chloride indicated that the aequorin transformed to the apoaequorin.
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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/Aequorin,
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Buffers,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/apoaequorin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0743-7463
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7602-7
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pubmed:meshHeading |
pubmed-meshheading:17555338-Aequorin,
pubmed-meshheading:17555338-Air,
pubmed-meshheading:17555338-Apoproteins,
pubmed-meshheading:17555338-Buffers,
pubmed-meshheading:17555338-Calcium Chloride,
pubmed-meshheading:17555338-Hydrogen-Ion Concentration,
pubmed-meshheading:17555338-Luminescent Agents,
pubmed-meshheading:17555338-Potassium Chloride,
pubmed-meshheading:17555338-Protein Structure, Secondary,
pubmed-meshheading:17555338-Recombinant Proteins,
pubmed-meshheading:17555338-Spectrometry, Fluorescence,
pubmed-meshheading:17555338-Spectrophotometry, Ultraviolet,
pubmed-meshheading:17555338-Surface Properties,
pubmed-meshheading:17555338-Water
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pubmed:year |
2007
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pubmed:articleTitle |
Surface properties of "jellyfish": Langmuir monolayer and Langmuir-Blodgett film studies of recombinant aequorin.
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pubmed:affiliation |
Department of Chemistry, University of Miami, Coral Gables, Florida 33146, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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