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Volumn 40, Issue 7, 2001, Pages 1976-1983
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Deletion of the helical motif in the intestinal fatty acid-binding protein reduces its interactions with membrane monolayers: Brewster angle microscopy, IR reflection-absorption spectroscopy, and surface pressure studies
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Author keywords
[No Author keywords available]
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Indexed keywords
1,2 DIMYRISTOYLPHOSPHATIDIC ACID;
AMPHOLYTE;
DIPALMITOYLPHOSPHATIDYLCHOLINE;
FATTY ACID;
FATTY ACID BINDING PROTEIN;
UNCLASSIFIED DRUG;
ABSORPTION SPECTROSCOPY;
ADSORPTION;
ARTICLE;
ELECTRICITY;
FATTY ACID TRANSPORT;
INFRARED SPECTROSCOPY;
MICROSCOPY;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN INTERACTION;
PROTEIN SECONDARY STRUCTURE;
RIGIDITY;
SPECTROSCOPY;
SURFACE PROPERTY;
AMINO ACID SEQUENCE;
ANIMALS;
CARBOHYDRATE CONFORMATION;
CARRIER PROTEINS;
FATTY ACID-BINDING PROTEINS;
FATTY ACIDS;
GLYCEROPHOSPHOLIPIDS;
HELIX-TURN-HELIX MOTIFS;
MEMBRANE LIPIDS;
MICROSCOPY;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
NEOPLASM PROTEINS;
NERVE TISSUE PROTEINS;
PROTEIN STRUCTURE, SECONDARY;
RATS;
SEQUENCE DELETION;
SPECTROPHOTOMETRY, INFRARED;
SURFACE PROPERTIES;
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EID: 0035916274
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002252i Document Type: Article |
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Times cited : (37)
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References (29)
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