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Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro.
 
Creator Kumar, Rajesh
Sharma, Deepak
Kumar, Vinay
Kumar, Rajesh
 
Subject QR Microbiology
 
Description The role of crowding agents on structure and activities of heme proteins has been established. Analysis of kinetic and thermodynamic parameters measured for CO-dissociation reaction of natively-folded carbonmonoxycytochrome c (NCO) and carbonmonoxymyoglobin (MbCO) at different [GdnHCl] or [Urea] in the presence of crowding agents (dextran 40, dextran 70 and ficoll 70) demonstrate that (i) at low denaturant concentrations, crowder presence enhances the denaturant-mediated restricted dynamics of NCO and MbCO, and (ii) at higher denaturant concentrations, large scale unfolding-fluctuations dominate the dynamics and inclusion of crowder counteracts the structural-fluctuations causing the unfolding of proteins. Thermodynamic analysis of thermal and urea-unfolding curves of cytochrome c (Cyt c) and myoglobin (Mb) measured at different [GdnHCl] in presence of crowding agents reveals that crowder presence counterbalances and strengthens the destabilizing action of GdnHCl on stability of Cyt c and Mb, respectively. This study further demonstrates that the size, shape and concentration of crowding agent modulate the effect of crowder on denaturant-mediated dynamics and thermodynamic stability of heme proteins.
 
Publisher Elsevier Science
 
Date 2018-09-15
 
Type Article
PeerReviewed
 
Relation https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(18)30213-3
http://crdd.osdd.net/open/2160/
 
Identifier Kumar, Rajesh and Sharma, Deepak and Kumar, Vinay and Kumar, Rajesh (2018) Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro. Archives of biochemistry and biophysics, 654. pp. 146-162. ISSN 1096-0384