AMINO-ACID-SEQUENCE PREFERENCES OF THE SALT-INDUCED PEPTIDE FORMATIONREACTION IN COMPARISON TO ARCHAIC CELL PROTEIN-COMPOSITION

Citation
Bm. Rode et al., AMINO-ACID-SEQUENCE PREFERENCES OF THE SALT-INDUCED PEPTIDE FORMATIONREACTION IN COMPARISON TO ARCHAIC CELL PROTEIN-COMPOSITION, Inorganica Chimica Acta, 254(2), 1997, pp. 309-314
Citations number
21
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
ISSN journal
00201693
Volume
254
Issue
2
Year of publication
1997
Pages
309 - 314
Database
ISI
SICI code
0020-1693(1997)254:2<309:APOTSP>2.0.ZU;2-E
Abstract
The salt-induced peptide formation (SIPF) reaction has been applied to a number of not yet investigated amino acids, leading to an overview of preferred peptide linkages resulting from this reaction, which is a t present the simplest and most universal known possibility of a prebi otic peptide formation in chemical evolution. These relative preferenc es of linkages in the SIPF reaction have been compared with the relati ve occurrence of amino acid pairing in the proteins of archaebacteria and prokaryotic cells. The similarity resulting from this comparison l ends strong support to the assumption that salt-induced peptide format ion may have supplied the basic units for the construction of protein precursors for the first primitive cells in evolution.