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Effects of Trimethylamine-N-oxide on the Conformation of Peptides and its Implications for Proteins

Zhaoqian Su, Farbod Mahmoudinobar, and Cristiano L. Dias
Phys. Rev. Lett. 119, 108102 – Published 8 September 2017
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Abstract

To provide insights into the stabilizing mechanisms of trimethylamine-N-oxide (TMAO) on protein structures, we perform all-atom molecular dynamics simulations of peptides and the Trp-cage miniprotein. The effects of TMAO on the backbone and charged residues of peptides are found to stabilize compact conformations, whereas effects of TMAO on nonpolar residues lead to peptide swelling. This suggests competing mechanisms of TMAO on proteins, which accounts for hydrophobic swelling, backbone collapse, and stabilization of charge-charge interactions. These mechanisms are observed in Trp cage.

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  • Received 23 February 2017

DOI:https://doi.org/10.1103/PhysRevLett.119.108102

© 2017 American Physical Society

Physics Subject Headings (PhySH)

Physics of Living SystemsPolymers & Soft Matter

Authors & Affiliations

Zhaoqian Su, Farbod Mahmoudinobar, and Cristiano L. Dias*

  • Physics Department, New Jersey Institute of Technology, Newark, 07102-1982 New Jersey, USA

  • *cld@njit.edu

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Issue

Vol. 119, Iss. 10 — 8 September 2017

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