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Thermodynamic analysis of partially folded states of myoglobin in presence of 2,2,2-trifluoroethanol

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Title Thermodynamic analysis of partially folded states of myoglobin in presence of 2,2,2-trifluoroethanol
 
Creator TALELE, P
KISHORE, N
 
Subject MOLTEN GLOBULE STATE
BOVINE ALPHA-LACTALBUMIN
CYTOCHROME-C
STRUCTURAL-CHARACTERIZATION
SECONDARY-STRUCTURE
PROTEIN
BINDING
TRIFLUOROETHANOL
APOMYOGLOBIN
NMR
Molten globule state
Myoglobin
2,2,2-Trifluoroethanol (TFE)
Isothermal titration calorimetry
Spectroscopy
8-Anilino-1-naphthalenesulfonic acid (ANS)
 
Description The thermal denaturation of myoglobin was studied in the presence of 2,2,2-trifluoroethanol (TFE) at various pH values using differential scanning calorimetry and UV-visible spectroscopy. The most obvious effect of TFE was lowering the transition temperature up to 1.5 mol . kg (1), beyond which no thermal transitions were observed. The protein conformation was analysed by fluorescence and circular dichroism measurements. Quantitative binding of ANS to the TFE induced molten globule state of myoglobin was studied by using isothermal titration calorimetry. The results enable quantitative estimation of the binding strength of ANS with the molten globule state of myoglobin along with the enthalpic and entropic contributions to the binding process. The results suggest occurrence of common structural features of the molten globule states of proteins offering two types of binding sites to ANS molecules which are a widely used fluorescence probe to characterise partially folded states of proteins. (C) 2014 Elsevier Ltd. All rights reserved.
 
Publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
 
Date 2016-01-14T14:19:25Z
2016-01-14T14:19:25Z
2015
 
Type Article
 
Identifier JOURNAL OF CHEMICAL THERMODYNAMICS, 84,50-59
0021-9614
1096-3626
http://dx.doi.org/10.1016/j.jct.2014.12.019
http://dspace.library.iitb.ac.in/jspui/handle/100/17710
 
Language en