Abstract
The correlation between various amino acid residues (either same or different), along the polypeptide chain have been studied using a large data base. A table of preference values for pairs having strong correlations has been constructed, which can be used to study any sequence and by calculating the weight of these sequences based on these preference values, a rough distinction between a “natural” and a “random” sequence can be made, One can further comment on the evolutionary status of proteins based on these weights.
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References
Anfinsen C B 1973 Principles that govern the folding of protein chains;Science 181 223–230
Kendall M 1976Time series, 2nd edition (London: Charles Griffin)
Kendall M, Stuart A and Ord J K 1983The advanced theory of statistics, 4th edition (London, High Wycombe: Charles Griffin)
Meeta Rani 1990Fractal dimensions of protein sequences, M.Phil Dissertation, University of Hyderabad, Hyderabad
Ptitsyn O B 1984 Proteins as edited polymers;Mol. Biol. USSR 18 574–590
Simon I 1985 Investigation of protein refolding: a special feature of native structure responsible for refolding ability;J. Theor. Biol. 113 703–710
Vonderviszt F, Matrai Gy and Simon I 1986 Characteristic residue environment of amino acid residues;Int. J. Pep. Prot. Res. 27 483–492
Mitra C K and Meeta Rani 1993Protein sequences as random fractals;J. Biosci. 18 213–220
Beran J 1992 Statistical methods for data with long range dependence;Stat. Sci. 7 404–427
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Rani, M., Mitra, C.K. Periodicities in protein sequences. J. Biosci. 19, 255–266 (1994). https://doi.org/10.1007/BF02703059
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DOI: https://doi.org/10.1007/BF02703059