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The Response of Water to Surface Structure is Key to Understanding Protein Self-Assembly on Mica

January 12, 2023

Alberstein et al Highlight Graphic_JPC Lett.JPG

Water's distinct response to substantially similar micas. Images show simulated water density at two different heights above the mica surface.

Scientific Achievement

Discovered that dramatic changes in protein organization seen on different types of mica surfaces arise from disparities in interfacial water structure associated with subtle differences in mica lattice structure.

Significance and Impact

The results show that the response of water to the mica surface changes dramatically with the sub-Å shifts in atomic positions, providing a rationale for observed differences in protein assembly on distinct types of mica. This finding upends previous understanding and has profound implications for design of protein-materials interfaces.

Research Details

  • We performed detailed molecular simulations of the intrinsic response of aqueous electrolytes to different forms of mica

  • We corroborated our findings by comparing the predictions to in situ atomic force microscopy maps of 3D water structure and images of protein assembly on mica

Alberstein, R., J. Prelesnik, E. Nakouzi, S. Zhang, J.J. De Yoreo, J. Pfaendtner, F.A. Tezcan, and C.J. Mundy. (2023). Discrete orientations of interfacial waters direct crystallization of mica-binding proteins. J. Phys. Chem. Lett. 14: 80-87. DOI: 10.1021/acs.jpclett.2c02948

Work performed at Pacific Northwest National Laboratory, the University of California San Diego, and the University of Washington.

Thrust 1: Emergence of Order: Research


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