Exploring conformational preferences of proteins: ionic liquid effects on the energy landscape of avidin.

ABSTRACT: In this work we experimentally investigate solvent and temperature induced conformational transitions of proteins and examine the role of ion-protein interactions in determining the conformational preferences of avidin, a homotetrameric glycoprotein, in choline-based ionic liquid (IL) solutions. Avidin was modified by surface cationisation and the addition of anionic surfactants, and the structural, thermal, and conformational stabilities of native and modified avidin were examined using dynamic light scattering, differential scanning calorimetry, and thermogravimetric analysis experiments. The protein-surfactant nanoconjugates showed higher thermostability behaviour compared to unmodified avidin, demonstrating distinct conformational ensembles. Small-angle X-ray scattering data showed tha

SUBMITTER: Shmool TA 

PROVIDER: S-EPMC8178808 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature