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Structural, kinetic and thermodynamic characterizations of SDS-induced molten globule state of a highly negatively charged cytochrome c.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Structural, kinetic and thermodynamic characterizations of SDS-induced molten globule state of a highly negatively charged cytochrome c.
 
Creator Jain, Rishu
Sharma, Deepak
Kumar, Rakesh
Kumar, Rajesh
 
Subject QR Microbiology
 
Description This study presents the structural, kinetic and thermodynamic characterizations of previously unknown submicellar concentrations of SDS-induced molten globule (MGSDS) state of a highly negatively charged base-denatured ferricytochrome c (UB-state) at pH ∼12.8 (±0.2). The far-UV CD, near-UV CD, ANS-fluorescence data of UB-state in the presence of different concentrations of SDS indicate that the submicellar concentrations of SDS (≤0.4 mM) transform the UB-state to MGSDS-state. The MGSDS-state has native-like α-helical secondary structure but lacks tertiary structure. The free energy change (ΔG°D) for UB→ MGSDS transition determined by far-UV CD (∼2.7 kcal mol-1) is slightly higher than those determined by fluorescence (∼2.0 kcal mol-1) at 25°C. At very low SDS and NaCl concentrations, the MGSDS-state undergoes cold denaturation. As SDS concentration is increased, the thermal denaturation temperature increases and the cold denaturation temperature decrease. Kinetic experiments involving the measurement of the CO-association rate to the base-denatured ferrocytochrome c at pH ≈12.8 (±0.2), 25°C indicate that the submicellar concentrations of SDS restrict the internal dynamics of base-denatured protein.
 
Publisher Oxford University Press
 
Date 2019-02-01
 
Type Article
PeerReviewed
 
Relation https://academic.oup.com/jb/article/165/2/125/5146343
http://crdd.osdd.net/open/2182/
 
Identifier Jain, Rishu and Sharma, Deepak and Kumar, Rakesh and Kumar, Rajesh (2019) Structural, kinetic and thermodynamic characterizations of SDS-induced molten globule state of a highly negatively charged cytochrome c. Journal of biochemistry, 165 (2). pp. 125-137. ISSN 1756-2651