FT-Raman spectroscopy in the metallothioneins: secondary structures and folding process

摘要

The folding process and motive force of proteins have been a research focus in Molecular Biology and Protein Engineering for several decades [1]. Among the several models brought up so far, one promising theory indicates that the folding of certain proteins is motivated by the special bonding effect of the sulful containing amino acid, Cys, to form sulfur-sulfur or sulfur-metal covalence [2]. However, no direct changes in the structures of sulfur containing groups during folding have been reported. Here, FT-Raman spectroscopy, a sensitive method to investigate the secondary structures and sulfur containing covalence of proteins was used to study the folding process of a Cys rich protein-metallothionein (MT).