Proteins as special subsets of polypeptides

Meeta Rani, Chanchal K. Mitra, M. Cserzo, I. Simon

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A large protein sequence database with over 31,000 sequences and 10 million residues has been analysed. The pair probabilities have been converted to entropies using Boltzmann's law of statistical thermodynamics. A scoring weight corresponding to "mixing entropy" of the amino acid pairs has been developed from which the entropies of the protein sequences have been calculated. The entropy values of natural sequences are lower than their random counterparts of same length and similar amino acid composition. Based on the results it has been proposed that natural sequences are a special set of polypeptides with additional qualification of biological functionality that can be quantified using the entropy concept as worked out in this paper.

Original languageEnglish
Pages (from-to)579-590
Number of pages12
JournalJournal of Biosciences
Volume20
Issue number5
DOIs
Publication statusPublished - Dec 1995

Fingerprint

Entropy
entropy
polypeptides
Peptides
Proteins
proteins
amino acid sequences
Amino Acids
Protein Databases
Statistical mechanics
Thermodynamics
amino acid composition
thermodynamics
Weights and Measures
amino acids
Chemical analysis

Keywords

  • mixing entropy
  • pair-preferences
  • Proteins
  • sequence analysis
  • statistical thermodynamics

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Proteins as special subsets of polypeptides. / Rani, Meeta; Mitra, Chanchal K.; Cserzo, M.; Simon, I.

In: Journal of Biosciences, Vol. 20, No. 5, 12.1995, p. 579-590.

Research output: Contribution to journalArticle

Rani, Meeta ; Mitra, Chanchal K. ; Cserzo, M. ; Simon, I. / Proteins as special subsets of polypeptides. In: Journal of Biosciences. 1995 ; Vol. 20, No. 5. pp. 579-590.
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