Diffusion in simple fluids

Speedy, Robin J.; Prielmeier, F. X.; Vardag, T.; Lang, Elmar; Lüdemann, H.‐D.

doi:10.1080/00268978900100341

Cited by 119 publications

(64 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Further justification of this f value can be found in the work of Speedy et al (1989). Moreover, a slightly different value of f (e.g., f=1) does not result in significantly different results.…”

Section: Repulsive Contribution To the Crowding Free Energymentioning

confidence: 89%

Protein–protein interactions in a crowded environment

2013

View full text Add to dashboard Cite

Protein-protein interactions are important in many essential biological functions, such as transcription, translation, and signal transduction. Much progress has been made in understanding protein-protein association in dilute solution via experimentation and simulation. Cells, however, contain various macromolecules, such as DNA, RNA, proteins, among many others, and a myriad of non-specific interactions (usually weak) are present between these cellular constituents. In this review article, we describe the important developments in recent years that have furthered our understanding and even allowed prediction of the consequences of macromolecular crowding on protein-protein interactions. We outline the development of our crowding theory that can predict the change in binding free energy due to crowding quantitatively for both repulsive and attractive protein-crowder interactions. One of the most important findings from our recent work is that weak attractive interactions between crowders and proteins can actually destabilize protein complex formation as opposed to the commonly assumed stabilizing effect predicted based on traditional crowding theories that only account for the entropicexcluded volume effects. We also discuss the implications of macromolecular crowding on the population of encounter versus specific native complex.

show abstract

Section: Repulsive Contribution To the Crowding Free Energymentioning

confidence: 89%

Protein–protein interactions in a crowded environment

2013

View full text Add to dashboard Cite

show abstract

“…Nevertheless, compared to viscosity [2][3][4][5][6] or even more self diffusion [7][8][9][10], there is a lack of systematic studies of the amplitude of thermal conductivity of the Lennard-Jones fluid, even if some recent results have been published [11][12][13][14]. In particular, to the best of our knowledge, it only exists one work (theoretically based) [14] which provides a relation to estimate the LJ thermal conductivity.…”

Section: Introductionmentioning

confidence: 99%

Thermal conductivity of the Lennard-Jones fluid: An empirical correlation

Bugel

Galliéro

2008

Chemical Physics

View full text Add to dashboard Cite

In this work, is presented an empirical correlation on the thermal conductivity of the Lennard-Jones fluid based on extensive non-equilibrium molecular dynamics simulations results (103 points). Finite size and cutoff radius effects are investigated and taken into account to develop the correlation. This last, composed of low density, residual and critical enhancement contributions, is built for a wide range of thermodynamics states, even at the vicinity of the critical point, and yields an average absolute deviation of 1.29 % compared to our simulations. In addition, a careful analysis of the different contributions to the microscopic flux is carried out which sheds light on the underlying mechanism of the results. Finally, are discussed the limitations of the proposed model when applied to real simple fluids and mixtures using a standard corresponding states scheme and the van der Waals one-fluid approximation.2

show abstract

“…Although this argument is simple, its experimental validity has been established for hundreds of fluids. 99 More recently, simulations of simple Lennard-Jones fluids in 2 and 3 dimensions have shown that ∆H a scales in proportion to the interaction parameter ε, [101][102][103] the natural measure of intermolecular interaction strength in simple pair potential models such as LJ fluids and also our polymer model.…”

Section: A Transition State Theorymentioning

confidence: 99%

A unifying framework to quantify the effects of substrate interactions, stiffness, and roughness on the dynamics of thin supported polymer films

Hanakata

Betancourt

Douglas

et al. 2015

The Journal of Chemical Physics

131

180

View full text Add to dashboard Cite

Changes in the dynamics of supported polymer films in comparison to bulk materials involve a complex convolution of effects, such as substrate interactions, roughness, and compliance, in addition to film thickness. We consider molecular dynamics simulations of substrate-supported, coarse-grained polymer films where these parameters are tuned separately to determine how each of these variables influence the molecular dynamics of thin polymer films. We find that all these variables significantly influence the film dynamics, leading to a seemingly intractable degree of complexity in describing these changes. However, by considering how these constraining variables influence string-like collective motion within the film, we show that all our observations can be understood in a unified and quantitative way. More specifically, the string model for glass-forming liquids implies that the changes in the structural relaxation of these films are governed by the changes in the average length of string-like cooperative motions and this model is confirmed under all conditions considered in our simulations. Ultimately, these changes are parameterized in terms of just the activation enthalpy and entropy for molecular organization, which have predictable dependences on substrate properties and film thickness, offering a promising approach for the rational design of film properties. C 2015 AIP Publishing LLC. [http://dx

show abstract

Diffusion in simple fluids

Cited by 119 publications

References 26 publications

Protein–protein interactions in a crowded environment

Protein–protein interactions in a crowded environment

Thermal conductivity of the Lennard-Jones fluid: An empirical correlation

A unifying framework to quantify the effects of substrate interactions, stiffness, and roughness on the dynamics of thin supported polymer films

Contact Info

Product

Resources

About