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Prion proteins: evolution and preservation of secondary structure
Author(s) -
Kuznetsov Igor B,
Morozov Pavel S,
Matushkin Yuri G
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00810-7
Subject(s) - phylogenetic tree , protein secondary structure , amino acid , prion proteins , protein evolution , prion protein , protein structure , computational biology , amino acid residue , chemistry , phylogenetics , biology , molecular evolution , genetics , evolutionary biology , peptide sequence , biochemistry , medicine , gene , pathology , disease
Prions cause a variety of neurodegenerative disorders that seem to result from a conformational change in the prion protein (PrP). Thirty‐two PrP sequences have been subjected to phylogenetic analysis followed by reconstruction of the most probable evolutionary spectrum of amino acid replacements. The replacement rates suggest that the protein does not seem to be very conservative, but in the course of evolution amino acids have only been substituted within the elements of the secondary structure by those with very similar physico‐chemical properties. Analysis of the full spectrum of single‐step amino acid substitutions in human PrP using secondary structure prediction algorithms shows an over‐representation of substitutions that tend to destabilize α‐helices.