Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: Spectroscopic description of the native, intermediate, and unfolded states

Biochimie

Volumn 89, Issue 11, 2007, Pages 1416-1424

  Nallamsetty, Sreedevi ^a   Dubey, Vikash K ^b   Pande, Monu ^a   Ambasht, P K ^a   Jagannadham, M V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

Cysteine proteases; Intermediate; Molten globule state; Stability

Indexed keywords

CYSTEINE PROTEINASE; ERVATAMIN A; UNCLASSIFIED DRUG; UREA;

ARTICLE; BETA SHEET; CHEMICAL STRUCTURE; CONCENTRATION (PARAMETERS); ENZYME STRUCTURE; MOLECULAR MODEL; MOLECULAR PROBE; PH; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROSCOPY; STRUCTURE ACTIVITY RELATION; TEMPERATURE; THERMOSTABILITY;

ANGIOSPERMS; BIOPHYSICS; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; ENZYME STABILITY; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS; ULTRAVIOLET RAYS; UREA;

TABERNAEMONTANA DIVARICATA;

EID: 35248888536     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.06.004     Document Type: Article

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