Journal
FEBS LETTERS
Volume 581, Issue 23, Pages 4377-4383Publisher
WILEY
DOI: 10.1016/j.febslet.2007.08.002
Keywords
molecular dynamics simulation; interfacial activation; hydrophobic effect; essential dynamics; alkane-aqueous interface; Candida rugosa lipase
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The effect of solvent hydrophobicity on activation of Candida rugosa lipase (CRL) was investigated by performing molecular dynamics simulations for four nano seconds (ns). The closed/inactive conformer of CRL (PDB code 1TRH) was solvated in three alkane-aqueous environments. The alkanes aggregated in a predominantly aqueous environment and by I ns a stable spherical alkane-aqueous interface had formed. This led to the interfacial activation of CRL. On analyzing the simulated conformers with the closed conformer of CRL, the flap was found to have opened from a closed state by 7.7 angstrom, 10.2 angstrom, 13.1 angstrom at hexane-aqueous, octane-aqueous, and decane-aqueous interfaces. Further, essential dynamics analysis revealed that major anharmonic fluctuations were confined to residues 64-81, the flap of CRL. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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