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  1. The aversion of hydrophobic solutes for water drives diverse interactions and assemblies across materials science, biology, and beyond. Here, we review the theoretical, computational, and experimental developments that underpin a contemporary understanding of hydrophobic effects. We discuss how an understanding of density fluctuations in bulk water can shed light on the fundamental differences in the hydration of molecular and macroscopic solutes; these differences, in turn, explain why hydrophobic interactions become stronger upon increasing temperature. We also illustrate the sensitive dependence of surface hydrophobicity on the chemical and topographical patterns the surface displays, which makes the use of approximate approaches for estimating hydrophobicity particularly challenging. Importantly, the hydrophobicity of complex surfaces, such as those of proteins, which display nanoscale heterogeneity, can nevertheless be characterized using interfacial water density fluctuations; such a characterization also informs protein regions that mediate their interactions. Finally, we build upon an understanding of hydrophobic hydration and the ability to characterize hydrophobicity to inform the context-dependent thermodynamic forces that drive hydrophobic interactions and the desolvation barriers that impede them.
    Free, publicly-accessible full text available March 10, 2023
  2. Interactions between proteins lie at the heart of numerous biological processes and are essential for the proper functioning of the cell. Although the importance of hydrophobic residues in driving protein interactions is universally accepted, a characterization of protein hydrophobicity, which informs its interactions, has remained elusive. The challenge lies in capturing the collective response of the protein hydration waters to the nanoscale chemical and topographical protein patterns, which determine protein hydrophobicity. To address this challenge, here, we employ specialized molecular simulations wherein water molecules are systematically displaced from the protein hydration shell; by identifying protein regions that relinquish their waters more readily than others, we are then able to uncover the most hydrophobic protein patches. Surprisingly, such patches contain a large fraction of polar/charged atoms and have chemical compositions that are similar to the more hydrophilic protein patches. Importantly, we also find a striking correspondence between the most hydrophobic protein patches and regions that mediate protein interactions. Our work thus establishes a computational framework for characterizing the emergent hydrophobicity of amphiphilic solutes, such as proteins, which display nanoscale heterogeneity, and for uncovering their interaction interfaces.

  3. Guest Editors Arthi Jayaraman and Amish Patel introduce this themed collection of papers showcasing the latest research on the molecular design and engineering of bioinspired, biological and/or biomimetic materials.
  4. We introduce an accurate and efficient method for characterizing surface wetting and interfacial properties, such as the contact angle made by a liquid droplet on a solid surface, and the vapor–liquid surface tension of a fluid. The method makes use of molecular simulations in conjunction with the indirect umbrella sampling technique to systematically wet the surface and estimate the corresponding free energy. To illustrate the method, we study the wetting of a family of Lennard-Jones surfaces by water. For surfaces with a wide range of attractions for water, we estimate contact angles using our method, and compare them with contact angles obtained using droplet shapes. Notably, our method is able to capture the transition from partial to complete wetting as surface–water attractions are increased. Moreover, the method is straightforward to implement and is computationally efficient, providing accurate contact angle estimates in roughly 5 nanoseconds of simulation time.