Kinetic stability plays a dominant role in the denaturant-induced unfolding of Erythrina indica lectin

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 6, 2006, Pages 1021-1028

  Ghosh, Sujit ^a   Mandal, Dipak K ^a  

^a PRESIDENCY UNIVERSITY   (India)

Author keywords

Equilibrium denaturation; Erythrina indica lectin; Legume lectin; Thermodynamic and kinetic stability; Unfolding kinetics

Indexed keywords

CALCIUM ION; EDETIC ACID; LECTIN; MANGANESE; METAL ION; UREA;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ERYTHRINA; ERYTHRINA INDICA; FAST PROTEIN LIQUID CHROMATOGRAPHY; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE DEPENDENCE; THERMODYNAMICS; ULTRAVIOLET RADIATION;

CALCIUM; CIRCULAR DICHROISM; DIMERIZATION; ERYTHRINA; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNESIUM; PLANT LECTINS; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROPHOTOMETRY; TEMPERATURE; THERMODYNAMICS; ULTRAVIOLET RAYS;

ERYTHRINA VARIEGATA;

EID: 33745191165     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.03.011     Document Type: Article

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