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Volumn 40, Issue 24, 2001, Pages 7291-7300

The reversible two-state unfolding of a monocot mannose-binding lectin from garlic bulbs reveals the dominant role of the dimeric interface in its stabilization

(4) Bachhawat, K a Kapoor, M a Dam, T K a Surolia, A a

a INDIAN INSTITUTE OF SCIENCE (India)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; DIMERS; FLUORESCENCE; FREE ENERGY; MONOMERS; PROTEINS; SCANNING; SPECIFIC HEAT;

LECTINS;

POLYPEPTIDES;

DIMER; LECTIN;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; GARLIC; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; X RAY ANALYSIS;

ALLIUM SATIVUM; SATIVUM;

EID: 0035912854 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0027783 Document Type: Article

Times cited : (22)

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