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

Authors

Zhaoqian Su, New Jersey Institute of Technology
Farbod Mahmoudinobar, New Jersey Institute of Technology
Cristiano L. Dias, New Jersey Institute of Technology

Document Type

Article

Publication Date

9-8-2017

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.

Identifier

85029697214 (Scopus)

Publication Title

Physical Review Letters

External Full Text Location

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

e-ISSN

10797114

ISSN

00319007

PubMed ID

28949191

Issue

10

Volume

119

Recommended Citation

Su, Zhaoqian; Mahmoudinobar, Farbod; and Dias, Cristiano L., "Effects of Trimethylamine- N -oxide on the Conformation of Peptides and its Implications for Proteins" (2017). Faculty Publications. 9312.
https://digitalcommons.njit.edu/fac_pubs/9312