Lid opening and conformational stability of T1 Lipase is mediated by increasing chain length polar solvents.

ABSTRACT: The dynamics and conformational landscape of proteins in organic solvents are events of potential interest in nonaqueous process catalysis. Conformational changes, folding transitions, and stability often correspond to structural rearrangements that alter contacts between solvent molecules and amino acid residues. However, in nonaqueous enzymology, organic solvents limit stability and further application of proteins. In the present study, molecular dynamics (MD) of a thermostable Geobacillus zalihae T1 lipase was performed in different chain length polar organic solvents (methanol, ethanol, propanol, butanol, and pentanol) and water mixture systems to a concentration of 50%. On the basis of the MD results, the structural deviations of the backbone atoms elucidated the dynamic effect

SUBMITTER: Maiangwa J 

PROVIDER: S-EPMC5438581 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature