A Historical Perspective and Overview of Protein Structure Prediction View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2007

AUTHORS

John C. Wooley , Yuzhen Ye

ABSTRACT

Carrying on many different biological functions, proteins are all composed of one or more polypeptide chains, each containing from several to hundreds or even thousands of the 20 amino acids. During the 1950s at the dawn of modern biochemistry, an essential question for biochemists was to understand the structure and function of these polypeptide chains. The sequences of protein, also referred to as their primary structures, determine the different chemical properties for different proteins, and thus continue to captivate much of the attention of biochemists. As an early step in characterizing protein chemistry, British biochemist Frederick Sanger designed an experimental method to identify the sequence of insulin (Sanger et al., 1955). He became the first person to obtain the primary structure of a protein and in 1958 won his first Nobel Price in Chemistry. This important progress in sequencing did not answer the question of whether a single (individual) protein has a distinctive shape in three dimensions (3D), and if so, what factors determine its 3D architecture. However, during the period when Sanger was studying the primary structure of proteins, American biochemist Christian Anfinsen observed that the active polypeptide chain of a model protein, bovine pancreatic ribonuclease (RNase), could fold spontaneously into a unique 3D structure, which was later called native conformation of the protein (Anfinsen et al., 1954). Anfinsen also studied the refolding of RNase enzyme and observed that an enzyme unfolded under extreme chemical environment could refold spontaneously back into its native conformation upon changing the environment back to natural conditions (Anfinsen et al., 1961). By 1962, Anfinsen had developed his theory of protein folding (which was summarized in his 1972 Nobel acceptance speech): “The native conformation is determined by the totality of interatomic interactions and hence, by the amino acid sequence, in a given environment.” More... »

PAGES

1-43

Book

TITLE

Computational Methods for Protein Structure Prediction and Modeling

ISBN

978-0-387-33319-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-0-387-68372-0_1

DOI

http://dx.doi.org/10.1007/978-0-387-68372-0_1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029369924


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