Prediction of Protein Structure from Amino Acid Sequence
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.
KeywordsSecondary Structure Prediction Unknown Structure Protein Crystallography Regular Secondary Structure Protein Topology
Unable to display preview. Download preview PDF.
- Clocksin,W.F., and Mellish,C.S., 1981, “Programming in Prolog”,Springer Verlag.Google Scholar
- Cohen,F.E., Sternberg,M.J.E., and Taylor,W.K. 1982, J. Mol. Biol.Google Scholar
- Cohen,F.E., Abarbanel,R.M., Kuntz,I.D., and Fletterick,R.J., 1983, Bio chemistry, 21:4894–4904.Google Scholar
- Glover,I., Haneef,I., Pitts,J., Woods,S., Moss,D., Tickle,I. and Blundell,T.L., 1983, Biophysics, 22:293–304.Google Scholar
- Old,R.W. and Primrose, S.B., “Principles of Gene Manipulation”, 3rd edition, Blackwell Scientific, Oxford.Google Scholar