Surfactants are widely used to refold recombinant proteins that are produced as inclusion bodies in E. Coli. However, the microscopic details of the surfactant-assisted protein refolding processes are yet to be uncovered. In the present work, the authors aim to provide insights into the effect of hydrophobic interactions of a denatured protein with surfactant molecules on the refolding kinetics and equilibrium by using the Langevin dynamics for coarse-grained models. The authors have investigated the folding behavior of a -barrel protein in the presence of surfactants of different hydrophobicities and concentrations. It is shown that the protein folding process follows a “collapse-rearrangement” mechanism, i.e., the denatured protein first falls into a collapsed state before acquiring the native conformation. In comparison with the protein folding without surfactants, the protein-surfactant hydrophobic interactions promote the collapse of a denatured protein and, consequently, the formation of a hydrophobic core. However, the surfactants must be released from the hydrophobic core during the rearrangement step, in which the native conformation is formed. The simulation results can be qualitatively reproduced by experiments.
Skip Nav Destination
Article navigation
14 February 2007
Research Article|
February 12 2007
Molecular dynamics for surfactant-assisted protein refolding
Diannan Lu;
Diannan Lu
Department of Chemical Engineering,
Tsinghua University
, Beijing 100084, China
Search for other works by this author on:
Zheng Liu;
Zheng Liu
Department of Chemical Engineering,
Tsinghua University
, Beijing 100084, China
Search for other works by this author on:
Jianzhong Wu
Jianzhong Wu
Department of Chemical and Environmental Engineering,
University of California
, Riverside, California 92521
Search for other works by this author on:
J. Chem. Phys. 126, 064906 (2007)
Article history
Received:
May 15 2006
Accepted:
November 21 2006
Citation
Diannan Lu, Zheng Liu, Jianzhong Wu; Molecular dynamics for surfactant-assisted protein refolding. J. Chem. Phys. 14 February 2007; 126 (6): 064906. https://doi.org/10.1063/1.2409931
Download citation file:
Sign in
Don't already have an account? Register
Sign In
You could not be signed in. Please check your credentials and make sure you have an active account and try again.
Sign in via your Institution
Sign in via your InstitutionPay-Per-View Access
$40.00
Citing articles via
CREST—A program for the exploration of low-energy molecular chemical space
Philipp Pracht, Stefan Grimme, et al.
GPAW: An open Python package for electronic structure calculations
Jens Jørgen Mortensen, Ask Hjorth Larsen, et al.
DeePMD-kit v2: A software package for deep potential models
Jinzhe Zeng, Duo Zhang, et al.