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Volumn 431, Issue 2, 2004, Pages 215-223
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Fluoroalcohol-induced stabilization of the α-helical intermediates of lentil lectin: Implication for non-hierarchical lectin folding
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Author keywords
Acid unfolding; Circular dichroism; Lentil lectin; Molten globule state
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Indexed keywords
LECTIN;
ACIDITY;
ALPHA HELIX;
ARTICLE;
BETA SHEET;
CIRCULAR DICHROISM;
LENTIL;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DETERMINATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
STRUCTURE ANALYSIS;
THERMODYNAMICS;
ULTRAVIOLET SPECTROSCOPY;
CIRCULAR DICHROISM;
HYDROGEN-ION CONCENTRATION;
LECTINS;
PLANT LECTINS;
PROTEIN BINDING;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
SPECTROMETRY, FLUORESCENCE;
TRIFLUOROETHANOL;
TRYPSIN;
LENS CULINARIS;
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EID: 5644253028
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/j.abb.2004.07.029 Document Type: Article |
Times cited : (11)
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References (46)
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