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Form of growing strings
D Marenduzzo1, T X Hoang, F Seno
1Mathematics Institute, University of Warwick, Coventry CV4 7AL, England, United Kingdom.
Physical Review Letters
|October 4, 2005
Summary
Nascent polypeptide chains growing in vivo spontaneously form helical structures, particularly at their growing ends. Evolution has conserved this nonequilibrium growth signature in native proteins, favoring helical formation.
Area of Science:
- * Biophysics
- * Molecular Biology
- * Evolutionary Biology
Background:
- * Natural patterns often arise from simple dynamical principles.
- * Understanding protein folding and structure is crucial in molecular biology.
- * Nascent polypeptides undergo complex growth and folding processes in vivo.
Purpose of the Study:
- * To investigate the self-organization of growing polypeptide chains.
- * To model the formation of helical structures during protein synthesis.
- * To explore the evolutionary implications of nonequilibrium growth in protein structure.
Main Methods:
- * Simulation of a growing self-interacting string attached to a tracking origin.
- * Analysis of the dynamic growth ensemble and comparison to equilibrium ensembles.
- * Statistical analysis of native protein states, focusing on the C terminus.
Main Results:
- * Growing self-interacting strings develop pronounced helical structures at their growing ends.
- * The dynamic growth process shares features with equilibrium ensembles under stretching force.
- * Evolutionary analysis reveals the C terminus (growing end) retains signatures of this nonequilibrium phenomenon.
Conclusions:
- * Nonequilibrium growth dynamics naturally favor helical structures in nascent polypeptide chains.
- * Evolution has exploited these inherent growth properties to establish helical structures at the C terminus.
- * This provides a mechanism for how generic nonequilibrium processes influence biological structure formation.