Literature DB >> 1300996

[Hidden symmetry of peptide and protein primary structures].

G I Chipens, N G Ievina, E E Tsilinskis.   

Abstract

The internal symmetry of peptide chains was considered. To identify symmetrically located equivalent amino acids, the signatures method and the code of amino acid codon roots were applied. There was revealed the hidden symmetry of amino acid sequences of peptides and proteins as well as of their active centres. Amino acids having common codon roots in primary (and supposedly in the spatial "biologically active") molecular structures, are located symmetrically. Definition of local symmetry of peptide chains was proposed to use as one of the elements of complex analysis to determine location of molecular active centres.

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Year:  1992        PMID: 1300996

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN: 0132-3423


  2 in total

1.  Internal mirror symmetry of nucleotide sequences in genes encoding different families of proteins.

Authors:  A O Shpakov
Journal:  Dokl Biochem Biophys       Date:  2001 Mar-Apr       Impact factor: 0.788

2.  A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis.

Authors:  Vladimir V Egorov; Dmitry V Lebedev; Aram A Shaldzhyan; Alexey K Sirotkin; Andrey N Gorshkov; Olga A Mirgorodskaya; Natalia A Grudinina; Andrey V Vasin; Michael M Shavlovsky
Journal:  Prion       Date:  2014       Impact factor: 3.931

  2 in total

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