id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_6e5xjyxuozbznhzyjhkxqwm3qa	Erte Xi	Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context	2017.0	6	.pdf	application/pdf	6663	865	64	hydrophobicity of curved graphene sheets, self-assembled monolayers (SAMs) with chemical patterns, and mutants of the protein hydrophobin-II. Our results highlight the power of water density fluctuations-based measures to characterize the hydrophobicity of nanoscale surfaces and caution against the use of additive To study context-dependent hydrophobicity we use molecular dynamics (MD) simulations coupled with enhanced sampling methods (24, 25) to systematically displace water molecules can characterize protein hydrophobicity and reveal its dependence on curvature and chemical patterns at the nanoscale. also show that hydrophobic patches with variations in chemical pattern and topography, whether on self-assembled monolayers (SAMs) or on the surface of a protein, hydrophobin-II, (B) Compressibility of water in the first hydration shell normalized by its value near a flat graphene sheet, χ/χgraphene , as a function of the surface curvature, Sarupria S, Garde S (2009) Quantifying water density fluctuations and compressibility of hydration shells of hydrophobic solutes and proteins.	./cache/work_6e5xjyxuozbznhzyjhkxqwm3qa.pdf	./txt/work_6e5xjyxuozbznhzyjhkxqwm3qa.txt