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Equimolar mixture of 2,2,2-trifluoroethanol and 4-chloro-1-butanol is a stronger inducer of molten globule state: Isothermal titration calorimetric and spectroscopic studies

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Title Equimolar mixture of 2,2,2-trifluoroethanol and 4-chloro-1-butanol is a stronger inducer of molten globule state: Isothermal titration calorimetric and spectroscopic studies
 
Creator THOPPIL, AA
KISHORE, N
 
Subject bovine alpha-lactalbumin
egg-white lysozyme
ribonuclease-a
thermodynamics
intermediate
proteins
binding
4-chlorobutan-1-ol
denaturation
stability
molten globule
alpha-lactalbumin
lysozyme
isothermal titration calorimetry
spectroscopy
 
Description A mixture of 4-chloro-1-butanol and 2,2,2-Trifluoroethanol (TFE) has been used to generate Molten globule (MG) state of structurally homologous but functionally different proteins bovine alpha-lactalbumin and hen egg-white lysozyme. The thermal denaturation was done using UV-Visible spectroscopy. From UV-Visible profile, thermal transition was not observed beyond a particular concentration. There was an indication of molten globule state in case of alpha-lactalbumin from circular dichroism experiments. By intrinsic tryptophan fluorescence, acrylamide and potassium iodide quenching, 8-anilino-naphthalene sulfonic acid (ANS) binding and energy transfer studies the presence of molten globule state was confirmed. Quantitative characterization of MG state and determining the binding thermodynamics of ANS to the MG state was done using Isothermal Titration Calorimetry (ITC). Results show that alpha-lactalbumin exists in MG state at a particular concentration but lysozyme does not show features of MG state.
 
Publisher SPRINGER
 
Date 2011-08-29T12:33:29Z
2011-12-26T12:58:35Z
2011-12-27T05:48:48Z
2011-08-29T12:33:29Z
2011-12-26T12:58:35Z
2011-12-27T05:48:48Z
2007
 
Type Article
 
Identifier PROTEIN JOURNAL, 26(7), 507-516
1572-3887
http://dx.doi.org/10.1007/s10930-007-9092-1
http://dspace.library.iitb.ac.in/xmlui/handle/10054/12083
http://hdl.handle.net/10054/12083
 
Language en