Conformational plasticity of cryptolepain: Accumulation of partially unfolded states in denaturants induced equilibrium unfolding

Journal of Biotechnology

Volumn 131, Issue 4, 2007, Pages 404-417

  Pande, Monu ^a   Dubey, Vikash K ^b   Sahu, Vishal ^a   Jagannadham, Medicherla V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

Intermediate; Molten globule state; Serine proteases; Stability

Indexed keywords

GLOBULAR PROTEINS; MOLTEN GLOBULE STATES; SERINE PROTEASES;

BINDING ENERGY; CONFORMATIONS; DENATURATION; FLUORESCENCE MICROSCOPY; PH EFFECTS; PHASE EQUILIBRIA;

PROTEIN FOLDING;

CRYPTOLEPAIN; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; BINDING KINETICS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CRYPTOLEPIS; CRYPTOLEPIS BUCHANANI; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROPHOBICITY; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY; TEMPERATURE; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; GUANIDINE; HYDROGEN-ION CONCENTRATION; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; THERMODYNAMICS; UREA;

CRYPTOLEPIS BUCHANANI;

EID: 34648819988     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.08.006     Document Type: Article

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