Effect of alkyl alcohols on partially unfolded state of Proteinase K: Differential stability of α-helix and β-sheet rich regions of the enzyme

Biochimie

Volumn 91, Issue 8, 2009, Pages 951-960

  Tomar, Ritu ^a   Dubey, Vikash Kumar ^b   Jagannadham, M V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

Folding pathway; Isopropanol; Non native state; Organic solvent; Proteinase K

Indexed keywords

2 PROPANOL; ALCOHOL; ALKANOL; METHANOL; PROTEINASE K; SERINE PROTEINASE;

ALPHA HELIX; ARTICLE; BETA SHEET; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; FUNGUS; HYDROPHOBICITY; NONHUMAN; PH MEASUREMENT; PHASE TRANSITION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; TEMPERATURE MEASUREMENT;

2-PROPANOL; ALCOHOLS; ASCOMYCOTA; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPEPTIDASE K; ENZYME STABILITY; FLUORESCENT DYES; GUANIDINE; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS; TEMPERATURE; WATER;

FUNGI; TRITIRACHIUM ALBUM;

EID: 67649502325     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.04.013     Document Type: Article

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