FTIR Spectroscopic Study of the Secondary Structure of Globular Proteins in Aqueous Protic Ionic Liquids.

ABSTRACT: Protein misfolding is a detrimental effect which can lead to the inactivation of enzymes, aggregation, and the formation of insoluble protein fibrils called Amyloids. Consequently, it is important to understand the mechanism of protein folding, and under which conditions it can be avoided or mitigated. Ionic liquids (ILs) have previously been shown as capable of increasing or decreasing protein stability, depending on the specific IL, IL concentration and which protein. However, a greater range of IL-proteins need to be systematically explored to enable the development of structure-property relationships. In this work, the secondary structure of four proteins, lysozyme, trypsin, β-lactoglobulin and α-amylase, were studied in aqueous solutions of 10 protic ionic liquids (PILs) with 0-50 mol

SUBMITTER: Arunkumar R 

PROVIDER: S-EPMC6381012 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature