Regularities in the primary structure of proteins.

M. Cserzö, I. Simon

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

In this paper the latest protein database consisting of more than a million amino acids is analyzed to characterize the short range regularities in the primary structure. The amino acid distributions along the polypeptide chain and among the proteins have been studied first. Their influence on the amino acid pair statistics was taken into account. We are primarily interested in the distances of the covalent structure, where the amino acid pair frequencies show non-random characters. The amino acid pairs separated by at least 20 residues in the covalent structure exhibit an exact Gaussian distribution. We found that there is a range of non-random pairing in the covalent structure. We conclude that the pair preference characters are different for each of the 20 x 20 amino acid pairs. The range of the non-random pairing varies from pair to pair, and in most cases it does not extend beyond the 9th neighbour. The preferences of a certain pair in a certain position can not be derived from the character of that pair in another position. The preference values of 400 amino acid pairs are listed for up to the pairs in 9th neighbour position. Some fields of potential application of these data have also been discussed.

Original languageEnglish
Pages (from-to)184-195
Number of pages12
JournalInternational Journal of Peptide and Protein Research
Volume34
Issue number3
Publication statusPublished - Sep 1989

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Amino Acid Sequence
Amino Acids
Proteins
Protein Databases
Normal Distribution
Gaussian distribution
Statistics
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Regularities in the primary structure of proteins. / Cserzö, M.; Simon, I.

In: International Journal of Peptide and Protein Research, Vol. 34, No. 3, 09.1989, p. 184-195.

Research output: Contribution to journalArticle

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