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Volumn 40, Issue 40, 2001, Pages 12215-12219
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A new spectroscopic approach to examining the role of disulfide bonds in the structure and unfolding of soybean trypsin inhibitor
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Author keywords
[No Author keywords available]
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Indexed keywords
CIRCULAR DICHROISM (CD);
ABSORPTION SPECTROSCOPY;
CHEMICAL BONDS;
FOURIER TRANSFORM INFRARED SPECTROSCOPY;
THERMAL EFFECTS;
X RAY SPECTROSCOPY;
PROTEINS;
DISULFIDE;
PHOSPHINE DERIVATIVE;
TRIS(2 CARBOXYETHYL) PHOSPHINE;
TRYPSIN INHIBITOR;
UNCLASSIFIED DRUG;
ARTICLE;
CIRCULAR DICHROISM;
ENZYME ACTIVITY;
HYDRATION;
INFRARED SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
REDUCTION;
SPECTROSCOPY;
TEMPERATURE DEPENDENCE;
DISULFIDES;
ELECTRON PROBE MICROANALYSIS;
MOLECULAR STRUCTURE;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
SPECTROPHOTOMETRY, ULTRAVIOLET;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
TRYPSIN INHIBITOR, KUNITZ SOYBEAN;
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EID: 0035834110
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi010796u Document Type: Article |
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Times cited : (37)
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References (23)
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