Chain Refolding and Subunit Interactions in Enzyme Molecules Covalently Bound to a Solid Matrix

Abstract

The biological and chemical properties of functionally active proteins are dependent upon their three-dimensional molecular structures. Insight into the role of the gene-determined primary sequence of a protein molecule in providing a thermodynamically stable tertiary structure with biological activity was obtained through the classical experiments of White, Anfinsen, and their colleagues on the renaturation of reductively denatured ribonuclease A (1–3). In these and subsequent investigations, it has been demonstrated that the acquisition of functional tertiary structures in relatively simple, single-chained protein molecules can occur spontaneously as a result of the inherent thermodynamics of the system; i.e., interactions among the linear array of amino acid residues and the molecular environment.

This investigation has been supported by National Science Foundation grant GI-39208. Paper 4206 of the Journal Series of the N. C. State University Agricultural Experiment Station, Raleigh, N. C.