From polymer configuration and dynamics to protein folding

Abstract

The force acting on the first bond of a polymer brush directly connected to a surface is low at high graftingdensities, at which nonvanishing end-monomer tension can be observed. The physical properties and variable applications ofthe polymers are determined based on their conformations and transition dynamics. As biological polymers, biomacromolecularproteins include twenty types of amino acids that form a linear polypeptide chain. Most proteins have a stablethree-dimensional native structure because of their one-dimensional amino acid sequences. In this review, we introduce apolymer brush, polymer nanocomposite materials, a polymer network, and their conformational transition dynamics along withthe conformation and folding and unfolding processes of the proteins. The folding and unfolding rates of proteins areregulated by the stretching force. The free energy and folding pathways of proteins can be studied in detail based on themeasurement of the force-dependent folding and unfolding rates of proteins. Furthermore, we consider the muscle proteintitin immunoglobulin domain I27 as an example to demonstrate the investigation of the protein folding and unfolding dynamicsusing single molecular manipulation techniques.