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Volumn 41, Issue 9, 2002, Pages 1546-1548
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The mechanical properties of human angiostatin can be modulated by means of its disulfide bonds: A single-molecule force-spectroscopy study
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Author keywords
Proteins; Reduction; Scanning probe microscopy; Single molecule studies
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Indexed keywords
REDOX ENVIRONMENT;
CHEMICAL BONDS;
DATA REDUCTION;
MECHANICAL PROPERTIES;
SPECTROSCOPIC ANALYSIS;
TOPOLOGY;
SULFUR COMPOUNDS;
ANGIOSTATIN;
DITHIOTHREITOL;
PLASMINOGEN;
POLYSTYRENE;
SODIUM CHLORIDE;
ARTICLE;
DISULFIDE BOND;
HUMAN;
HYDROPHOBICITY;
KRINGLE DOMAIN;
MECHANICS;
PROTEIN FOLDING;
PROTEIN STRUCTURE;
SCANNING FORCE MICROSCOPY;
SEQUENCE HOMOLOGY;
SPECTROSCOPY;
ANGIOSTATINS;
DISULFIDES;
HUMANS;
MECHANICAL PHENOMENA;
MODELS, MOLECULAR;
PROTEIN CONFORMATION;
SPECTRUM ANALYSIS;
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EID: 0037012705
PISSN: 14337851
EISSN: None
Source Type: Journal
DOI: 10.1002/1521-3773(20020503)41:9<1546::AID-ANIE1546>3.0.CO;2-U Document Type: Article |
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Times cited : (22)
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References (17)
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