Prediction of Protein Structure from Amino Acid Sequence

  • Michael J. E. Sternberg
Part of the NATO ASI Series book series (NSSA, volume 126)


Renaturation experiments show that a folded active protein can be unfolded and inactivated and then this process can be reversed to yield the active folded molecule. Thus it is considered that the amino acid sequence and the protein environment determine the three-dimensional conformation of a protein. Accordingly workers are trying to predict theoretically the three-dimensional structure of a protein from its sequence. Prediction will be useful as protein crystallography is at best time-consuming (typically at least 10 man years) and sometimes impossible because of unsuitable or unavailable crystals. In contrast, amino acid sequence information, today often derived from the nucleic acid sequence, is becoming available for many proteins. Recently, the advent of protein engineering has increased the requirements to model the relationship between protein sequence and conformation (eg. Fersht et al, 1985). This paper reviews available methods of structure prediction and introduces developments using data bases and logic programming computer languages.


Secondary Structure Prediction Unknown Structure Protein Crystallography Regular Secondary Structure Protein Topology 


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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • Michael J. E. Sternberg
    • 1
  1. 1.Department of CrystallographyBirkbeck CollegeLondonUK

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