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Prediction of Protein Structure and the Principles of Protein Conformation pp 647–705Cite as

Tertiary Structure Prediction

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Abstract

The polypeptide chain of globular protein is linear, but the three-dimensional of tertiary structure is quite contorted. This was apparent from the first crystallographic determination of the structure of a protein by Kendrew et al. (1960). The contortion arises because of the need to satisfy a multitude of conflicting interactions: the hydrogen-bonding requirements of buried nitrogen and oxygen atoms, placement of the remaining polar groups near the protein-solvent interface, and internalization of most hydrophobic residues. Anfinsen et al. (1961) demonstarted that the amino acid sequence contained enough information to define a protein tertiary structure. These experiments defined the protein-folding problem: by computation determine the precise tertiary structure of a protein from its amino acid sequence. In the 25 years that have followed, much regularity and order have been recognized in protein tertiary structure (for reviews, see Richards, 1977; Nemethy and Scherega, 1977; Schulz and Schirmer, 1979; Richardson, 1981; Sternberg, 1983; Chothia, 1984). This chapter describes some of the theoritical methods designed to predict protein structure.

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  1. Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California, 94143-04460, USA

    Fred E. Cohen & Irwin D. Kuntz

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  1. Fred E. Cohen
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  1. Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts, 02254, USA

    Gerald D. Fasman

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Cohen, F.E., Kuntz, I.D. (1989). Tertiary Structure Prediction. In: Fasman, G.D. (eds) Prediction of Protein Structure and the Principles of Protein Conformation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1571-1_17

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