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Compact phases of polymers with hydrogen bonding
Antonio Trovato1, Jesper Ferkinghoff-Borg, Mogens H Jensen
1INFM-Dipartimento di Fisica G. Galilei, Università di Padova, Via Marzolo 8, 35131 Padova, Italy.
Summary
This study models homopolymer chains with competing hydrophobic and hydrogen-bonding interactions. Results show helical structures dominate with strong hydrogen bonds, while weaker bonds favor compact beta-sheet-like conformations.
Area of Science:
- Computational chemistry
- Polymer physics
- Biophysics
Background:
- Homopolymer chains exhibit complex conformational behavior due to competing interactions.
- Understanding these interactions is crucial for modeling protein folding and self-assembly.
Purpose of the Study:
- To investigate the phase diagram of a self-avoiding homopolymer with competing hydrophobic and hydrogen-bonding interactions.
- To determine the influence of relative interaction strengths on chain conformation.
Main Methods:
- Development of an off-lattice model for homopolymer chains.
- Utilizing Monte Carlo simulations to explore the conformational space.
- Analysis of the complete phase diagram for varying interaction strengths.
Main Results:
- Strong hydrogen bonding stabilizes helical conformations as the ground state.
- Decreasing hydrogen-bonding strength leads to the destabilization of helices.
- At lower temperatures and weaker hydrogen bonding, compact beta-sheet-like structures emerge.
Conclusions:
- The balance between hydrophobic and hydrogen-bonding interactions dictates homopolymer folding pathways.
- Helical structures are favored under specific hydrogen-bonding conditions, while beta-sheet-like structures form under others.
- This model provides insights into the fundamental principles governing protein structure formation.