Critical Residue That Promotes Protein Dimerization: A Story of Partially Exposed Phe25 in 14-3-3σ

Abstract

Many proteins exist and function as oligomers. While hydrophobic interactions have been recognized as the major driving force for oligomerization, detailed molecular mechanisms for the assembly are unknown. Here, we used 14-3-3σ as a model protein and investigated the role of hydrophobic residues at the dimeric interface using MD simulations and… (More)
DOI: 10.1021/ci200212y

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Cite this paper

@article{Liu2011CriticalRT, title={Critical Residue That Promotes Protein Dimerization: A Story of Partially Exposed Phe25 in 14-3-3σ}, author={Jing-Yuan Liu and Zhaomin Li and Huian Li and Jian-Ting Zhang}, journal={Journal of chemical information and modeling}, year={2011}, volume={51 10}, pages={2612-25} }