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Ricercatore a tempo determinato di tipo b senior in Chimica Organica
Università di Pisa
Dipartimento di Chimica e Chimica Industriale
via Moruzzi, 13
56124 Pisa

website: http://www.sosandpepsy.org/
e-mail: gaetano.angelici@unipi.it

 

 

 

“Many naturally-occurring proteins fold reliably  and quickly to their native state despite the  astronomical number of  possible configurations. In nature, proteins apparently do not sample all  of these possible  configurations since they fold in a few seconds, and even postulating minimum  time for going from one  conformation to another, the proteins would have time to try on the order of 108 different conformations at most before reaching their final state.

We feel that protein folding is speeded and guided  by the rapid formation of local interactions which then determine  the further folding of the peptide.  This suggests local amino acid  sequences which form stable interactions and serve as nucleation points in the folding process.”

 

               -C. Levinthal, Journal de Chimie Physique et de Physico-Chimie Biologique, 1968, 65, 44–45