Free energies and equilibria of peptide bond hydrolysis and formation

✍ Scribed by R. Bruce Martin

• Publisher: Wiley (John Wiley & Sons)
• Year: 1998
• Tongue: English
• Weight: 40 KB
• Volume: 45
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(19980415)45:5<351::aid-bip3>3.0.co;2-k

✦ Synopsis

For every n amino acids linked in a protein there are n 0 1 peptide bonds. The free energy of peptide bond hydrolysis and formation in aqueous solution defines the equilibrium position between peptide and amino acid hydrolysis products. Yet few experimental values exist. With a minimum of assumptions, this paper deduces the free energies of hydrolysis of a variety of peptide bonds. Formation of a dipeptide from two amino acids is about eight times more difficult than subsequent condensations of an amino acid to a dipeptide or longer chain. Condensation of an amino acid to a peptide of any size is five times more difficult than joining two smaller peptides of at least dipeptide size. Thus in an abiogenesis scenario there is a kind of nucleation in peptide bond formation with the initial condensation of two amino acids to yield a dipeptide more difficult than subsequent condensations to a growing chain.