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The adsorption of a collagen fragment on both a hydrophobic, hydrogen-terminated and a hydrophilic, natively oxidised Si surface is investigated using all-atom molecular dynamics. While favourable direct protein-surface interactions via…

Soft Condensed Matter · Physics 2019-03-27 Daniel J. Cole , Mike C. Payne , Lucio Colombi Ciacchi

Using coarse grained models we investigate the behavior of water adjacent to an extended hydrophobic surface peppered with various fractions of hydrophilic patches of different sizes. We study the spatial dependence of the mean interface…

Statistical Mechanics · Physics 2014-09-09 Adam P. Willard , David Chandler

Solvent often manifests itself as the key determinant of the kinetic aspect of molecular recognition process. While the solvent is often depicted as a source of barrier in the ligand recognition process by polar cavity, the nature of…

Chemical Physics · Physics 2020-03-18 Navjeet Ahalawat , Satyabrata Bandyopadhyay , Jagannath Mondal

We present a coarse-grained model for ionic surfactants in explicit aqueous solutions, and study by computer simulation both the impact of water content on the morphology of the system, and the consequent effect of the formed interfaces on…

Soft Condensed Matter · Physics 2015-03-16 Samuel Hanot , Sandrine Lyonnard , Stefano Mossa

Unstructured proteins can modulate cellular responses to environmental conditions by undergoing coil-globule transitions and phase separation. However, the molecular mechanisms of these phenomena still need to be fully understood. Here, we…

Soft Condensed Matter · Physics 2023-06-28 Bernat Durà Faulí , Valentino Bianco , Giancarlo Franzese

Adsorption of small amphiphilic molecules occurs in various biological and technological processes, sometimes desired, the other times unwanted (e.g., contamination). Surface-active molecules preferentially bind to interfaces and affect…

Soft Condensed Matter · Physics 2022-11-24 Fabio Staniscia , Horacio V. Guzman , Matej Kanduč

The influence of the patchiness and correlations in the distribution of hydrophobic and polar residues at the interface between two rigid biomolecules on their recognition ability is investigated in idealised coarse-grained lattice models.…

Biological Physics · Physics 2009-11-13 Hans Behringer , Friederike Schmid

The influence of the external pressure and surface energy on the wetting transition at nanotextured interfaces is studied using molecular dynamics and continuum simulations. The surface roughness of the composite interface is introduced via…

Soft Condensed Matter · Physics 2018-07-12 Bishal Bhattarai , Nikolai V. Priezjev

Water and water-mediated interactions determine thermodynamic and kinetics of protein folding, protein aggregation and self-assembly in confined spaces. To obtain insights into the role of water in the context of folding problems, we…

Soft Condensed Matter · Physics 2015-05-28 S. Vaitheeswaran , Jie Chen , D. Thirumalai

The density of a protein molecule is a key property within a variety of experimental techniques. We present a computational method for determining protein mass density that explicitly incorporates hydration effects. Our approach uses…

We study the dynamics of hydration water/protein association in folded proteins, using lysozyme and myoglobin as examples. Extensive molecular dynamics simulations are performed to identify underlying mechanisms of the dynamical transition…

Soft Condensed Matter · Physics 2015-05-13 J. Servantie , C. Atilgan , A. R. Atilgan

Water near hydrophobic surfaces is like that at a liquid-vapor interface, where fluctuations in water density are substantially enhanced compared to that in bulk water. Here we use molecular simulations with specialized sampling techniques…

Water is essential for the activity of proteins. However, the effect of the properties of water on the behavior of proteins is only partially understood. Recently, several experiments have investigated the relation between the dynamics of…

Biological Physics · Physics 2015-03-17 Giancarlo Franzese , Valentino Bianco , Svilen Iskrov

Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues tends to occur at the surface of a folded protein. By…

Biomolecules · Quantitative Biology 2007-05-23 Susanne Moelbert , Eldon Emberly , Chao Tang

We use molecular dynamics computer simulations and nuclear magnetic resonance experiments to investigate the dynamics of water at interfaces of molecular roughness and low mobility. We find that, when approaching such interfaces, the…

Soft Condensed Matter · Physics 2014-07-22 Markus Rosenstihl , Kerstin Kämpf , Felix Klameth , Matthias Sattig , Michael Vogel

Particles added to a fluid interface can be used as a surface stabilizer in the food, oil and cosmetic industries. As an alternative to rigid particles, it is promising to consider highly deformable particles that can adapt their…

Soft Condensed Matter · Physics 2016-10-27 Hadi Mehrabian , Jens Harting , Jacco H. Snoeijer

Clarifying the factors that control the contact angle of a liquid on a solid substrate is a long-standing scientific problem pertinent across physics, chemistry and materials science. Progress has been hampered by the lack of a…

Statistical Mechanics · Physics 2019-11-11 Robert Evans , Maria C. Stewart , Nigel B. Wilding

Proteins tend to bury hydrophobic residues inside their core during the folding process to provide stability to the protein structure and to prevent aggregation. Nevertheless, proteins do expose some 'sticky' hydrophobic residues to the…

Biomolecules · Quantitative Biology 2021-07-27 Juami Hermine Mariama van Gils , Dea Gogishvili , Jan van Eck , Robbin Bouwmeester , Erik van Dijk , Sanne Abeln

As a first step towards a microscopic understanding of the effective interaction between colloidal particles suspended in a solvent we study the wetting behavior of one-component fluids at spheres and fibers. We describe these phenomena…

Condensed Matter · Physics 2015-06-25 T. Bieker , S. Dietrich

We fit the Fourier transforms of solvent accessibility and hydrophobicity profiles of a representative set of proteins to a joint multi-variable Gaussian. This allows us to separate the intrinsic tendencies of sequence and structure…

Biomolecules · Quantitative Biology 2007-05-23 Mehdi Yahyanejad , Christopher B. Burge , Mehran Kardar