Large scale analysis of protein conformational transitions from aqueous to non-aqueous media.

ABSTRACT:

Background

Biocatalysis in organic solvents is nowadays a common practice with a large potential in Biotechnology. Several studies report that proteins which are co-crystallized or soaked in organic solvents preserve their fold integrity showing almost identical arrangements when compared to their aqueous forms. However, it is well established that the catalytic activity of proteins in organic solvents is much lower than in water. In order to explain this diminished activity and to further characterize the behaviour of proteins in non-aqueous environments, we performed a large-scale analysis (1737 proteins) of the conformational diversity of proteins crystallized in aqueous and co-crystallized or soaked in non-aqueous media.

Results

Using proteins' experimentally determined

SUBMITTER: Rueda AJV 

PROVIDER: S-EPMC5791380 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature