Considerations on the Tertiary Structure of Proteins

作者：H. K. Schachman · 发表于：Cold Spring Harbor Symposia on Quantitative Biology · 年份：1963 · DOI：10.1101/sqb.1963.028.01.057 · 被引用次数：77 · 研究领域：Protein Structure and Dynamics、Enzyme Structure and Function、Glycosylation and Glycoproteins Research

Current research in molecular genetics and protein biosynthesis has stimulated renewed interest in investigations of the folding of disorganized polypeptide chains to produce biologically active protein molecules with unique specificities and three-dimensional conformations. According to present views the characteristic secondary and tertiary structures of native protein molecules are the direct consequence of the sequential arrangement of the amino acids in the polypeptide chains. In support of this view, examples can be cited where the disorganized polypeptide chains produced by the denaturation of proteins were transformed readily into biologically active macromolecules having the properties and architecture characteristic of the native proteins.