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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/20700
Title: Mutation of the hydrophobic residue on helix α5 of the Bacillus thuringiensis Cry4B affects structural stability
Authors: Chartchai Krittanai
Apichai Bourchookarn
Wanwarang Pathaichindachote
Sakol Panyim
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 15-Aug-2003
Citation: Protein and Peptide Letters. Vol.10, No.4 (2003), 361-368
Abstract: Cry4B toxin is a mosquito-larvicidal protein from the Bacillus thuringiensis subsp. israelensis. We have investigated the role of two conserved hydrophobic residues of Cry4B in structural stabilization. Substitutions of the leucine-175 and isoleucine-189 on helix α5 with valine and leucine did not affect the expression level, solubility and proteolytic processing. Steady state analysis of an unfolding experiment as monitored by circular dichroism and fluorescence spectroscopy demonstrated a typical two-state transition. The determined unfolding free energy for the L175V mutant revealed a structural destabilization of 10.49 kcal/mol relative to the wild type. However unfolding kinetic analysis gave identical activation energy for wild type and both mutants. Our findings suggested that a perturbation on the close packing of the hydrophobic side chains in protein interior could lead to a significant destabilization of the native conformation.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0041703058&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/20700
ISSN: 09298665
Appears in Collections:Scopus 2001-2005

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