Fluoroalcohols induced unfolding of Succinylated Con A: Native like β-structure in partially folded intermediate and α-helix in molten globule like state

Archives of Biochemistry and Biophysics

Volumn 454, Issue 2, 2006, Pages 170-180

  Fatima, Sadaf ^a   Ahmad, Basir ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Circular dichroism; Molten globule like state; Partially folded intermediate; Succinylated Con A

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALCOHOL; AMYLOID; CONCANAVALIN A; DYE; FLUOROALCOHOL; HEXAFLUORO 2 PROPANOL; SUCCINIC ACID DERIVATIVE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; ELECTROCHEMISTRY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; CONCANAVALIN A; DIMERIZATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; HYDROPHOBICITY; MICROSCOPY, FLUORESCENCE; PROPANOLS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; TRIFLUOROETHANOL;

EID: 33749610128     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.08.014     Document Type: Article

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