ABSTRACT
Most cell wall and secreted ß-glucans are synthesised by the CAZy Glycosyltransferase 2 family (www.cazy.org), with different members catalysing the formation of (1,4)-ß-, (1,3)-ß-, or both (1,4)- and (1,3)-ß-glucosidic linkages. Given the distinct physicochemical properties of each of the resultant ß-glucans (cellulose, curdlan, and mixed linkage glucan, respectively) are crucial to their biological and biotechnological functions, there is a desire to understand the molecular evolution of synthesis and how linkage specificity is determined. With structural studies hamstrung by the instability of these proteins to solubilisation, we have utilised in silico techniques and the crystal structure for a bacterial cellulose synthase to further understand how these enzymes have evolved distinct functions. Sequence and phylogenetic analyses were performed to determine amino acid conservation, both family-wide and within each sub-family. Further structural analysis centred on comparison of a bacterial curdlan synthase homology model with the bacterial cellulose synthase crystal structure, with molecular dynamics simulations performed with their respective ß-glucan products bound in the trans-membrane channel. Key residues that differentially interact with the different ß-glucan chains and have sub-family-specific conservation were found to reside at the entrance of the trans-membrane channel. The linkage-specific catalytic activity of these enzymes and hence the type of ß-glucan chain built is thus likely determined by the different interactions between the proteins and the first few glucose residues in the channel, which in turn dictates the position of the acceptor glucose. The sequence-function relationships for the bacterial ß-glucan synthases pave the way for extending this understanding to other kingdoms, such as plants.
Subject(s)
Bacterial Proteins/chemistry , Glucosyltransferases/chemistry , beta-Glucans/metabolism , Amino Acid Sequence , Bacterial Proteins/metabolism , Catalytic Domain , Conserved Sequence , Glucosyltransferases/metabolism , Hydrogen Bonding , Models, Molecular , Phylogeny , Protein Conformation , Structure-Activity RelationshipABSTRACT
The interleukin-3 (IL-3) receptor is a cell-surface heterodimer that links the haemopoietic, vascular and immune systems and is overexpressed in acute and chronic myeloid leukaemia progenitor cells. It belongs to the type I cytokine receptor family in which the α-subunits consist of two fibronectin III-like domains that bind cytokine, and a third, evolutionarily unrelated and topologically conserved, N-terminal domain (NTD) with unknown function. Here we show by crystallography that, while the NTD of IL3Rα is highly mobile in the presence of IL-3, it becomes surprisingly rigid in the presence of IL-3 K116W. Mutagenesis, biochemical and functional studies show that the NTD of IL3Rα regulates IL-3 binding and signalling and reveal an unexpected role in preventing spontaneous receptor dimerisation. Our work identifies a dual role for the NTD in this cytokine receptor family, protecting against inappropriate signalling and dynamically regulating cytokine receptor binding and function.
Subject(s)
Interleukin-3 Receptor alpha Subunit/chemistry , Interleukin-3 Receptor alpha Subunit/metabolism , Protein Domains , Signal Transduction , Amino Acid Sequence , Animals , Binding Sites/genetics , COS Cells , Cell Line, Tumor , Chlorocebus aethiops , Crystallography, X-Ray , HEK293 Cells , Humans , Interleukin-3/chemistry , Interleukin-3/genetics , Interleukin-3/metabolism , Interleukin-3 Receptor alpha Subunit/genetics , Molecular Dynamics Simulation , Mutation , Protein BindingABSTRACT
There is increasing experimental and computational evidence that cellulose microfibrils can exist in a stable twisted form. In this study, atomistic molecular dynamics (MD) simulations are performed to investigate the importance of intrachain hydrogen bonds on the twist in cellulose microfibrils. We systematically enforce or block the formation of these intrachain hydrogen bonds by either constraining dihedral angles or manipulating charges. For the majority of simulations a consistent right handed twist is observed. The exceptions are two sets of simulations that block the O2-O6' intrachain hydrogen bond, where no consistent twist is observed in multiple independent simulations suggesting that the O2-O6' hydrogen bond can drive twist. However, in a further simulation where exocyclic group rotation is also blocked, right-handed twist still develops suggesting that intrachain hydrogen bonds are not necessary to drive twist in cellulose microfibrils.
ABSTRACT
Hydrodynamic interactions play an important role in the transport of analytes through nanoscale devices. Of particular note is the role that no-slip boundary conditions have on the drag coefficient of confined particles and molecules. In this work, we use a coarse grained molecular dynamics model to measure the diffusion coefficients of proteins confined within cylindrical nanochannels of similar dimension. Finite-size corrected bulk diffusion coefficients are found to agree with experimental data, while in channels, a good match is found between theoretical expressions based on continuum fluid mechanics and the reduction of the translational diffusion coefficient across a range of protein to channel size ratios. These results demonstrate that it is possible to directly use molecular simulation to make quantitative predictions of the effects of hydrodynamics on diffusion at length scales of order 1 nm.
Subject(s)
Proteins/chemistry , Diffusion , Humans , Hydrodynamics , Molecular Dynamics Simulation , Nanotubes/chemistry , Streptavidin/chemistry , Streptomyces/chemistry , Ubiquitin/chemistryABSTRACT
The free energy associated with transferring a set of fullerene particles through a finite water layer is calculated using explicit solvent molecular dynamic simulations. Each fullerene particle is a carbon network of one or more spheroidal shells of graphitic carbon, and include single-shell (single-wall) or nested multi-shelled (nano-onions) structures ranging from 6 to 28 Å in radius. Corresponding changes in energy suggest a stronger affinity of carbon nano-onions for water compared to their single-shelled analogues. In the case of multi-shelled structures, the free energy profiles display a global minimum only in the bulk liquid indicating a high affinity of multi-shelled fullerene for complete hydration. Single-wall particles however, display a minimum at the air-water interface and for particles larger than 2 nm this minimum is a global minimum possessing a lower energy compared to the particle's state of complete hydration. While the propensity for single-shell particles to adsorb to the air-interface may increase with increasing particle size, there is an indication based on line tension calculations that larger single-shell particles may actually exhibit enhanced wetting compared to their smaller analogues.
ABSTRACT
Nested fullerenes display a range of unique properties influenced by their size and shape. In this paper, the size- and shape-dependent aggregation of nested fullerenes in water is studied using explicit solvent molecular dynamic simulations. It is shown that water forms a layered structure near the surface of the particle, with the density of interfacial water increasing with increasing particle size. Meanwhile, water molecules near the extended facets of large nested fullerenes are unable to maintain their hydrogen bonding network, leading to a shape and size mediated structuring of surrounding waters. These distortions affect the overall association kinetics of particles in water with spherically shaped particles transitioning quickly into contact, while larger fullerenes, characterized by a lower sphericity, cluster at a much slower rate.
ABSTRACT
Dinuclear polypyridylruthenium(II) complexes bridged by a flexible methylene linker have received considerable interest as potential antibacterial agents. Their potency and uptake into bacterial cells is directly modulated by the length of the bridging linker, which has implicated membrane interactions as an essential feature of their mechanism of action. In this work, a combination of molecular dynamics (MD) simulations and solid-state NMR was used to present an atomistic model of a polypyridylruthenium(II) complex bound and incorporated into a bacterial membrane model. The results of 31P, 2H, 1H, and 13C NMR studies revealed that the antibacterial [{Ru(phen)2}2(µ-bb12)]4+ complex (Rubb12), where phen = 1,10-phenanthroline and bb12 = bis[4(4'-methyl-2,2'-bipyridyl)]-1,12-dodecane), incorporated into a negatively charged model bacterial membrane, but only associated with the surface of a charge-neutral model of a eukaryotic membrane. Furthermore, an inactive [{Ir(phen)2}2(µ-bb12)]6+ (Irbb12) analogue, which is not taken up by bacterial cells, maintained only a surface-bound association with both bacterial and eukaryotic model membranes according to 31P and 2H NMR. The effects of Rubb12 on 31P chemical shift anisotropy and 2H acyl chain order parameters for negatively charged membranes correlated with a membrane-spanning state of the complex according to MD simulation-in which the metal centers embed in the lipid head group region and the central void, created by the biconic shape of the complex, resulting in increasing disorder of lipid acyl chains and membrane-thinning. A transbilayer mechanism and membrane-spanning may be essential for the cellular uptake and antibacterial activity of this class of compounds.
Subject(s)
2,2'-Dipyridyl/pharmacology , Anti-Bacterial Agents/pharmacology , Molecular Dynamics Simulation , Polymers/pharmacology , Ruthenium/pharmacology , Staphylococcus aureus/drug effects , 2,2'-Dipyridyl/chemistry , Animals , Anti-Bacterial Agents/chemical synthesis , Anti-Bacterial Agents/chemistry , Cell Death/drug effects , Cell Line , Magnetic Resonance Spectroscopy , Mice , Microbial Sensitivity Tests , Polymers/chemical synthesis , Polymers/chemistry , Ruthenium/chemistry , Staphylococcus aureus/cytologyABSTRACT
Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step in the diaminopimelate pathway of bacteria, yielding amino acids required for cell wall and protein biosyntheses. The essentiality of the enzyme to bacteria, coupled with its absence in humans, validates DHDPS as an antibacterial drug target. Conventional drug design efforts have thus far been unsuccessful in identifying potent DHDPS inhibitors. Here, we make use of contemporary molecular dynamics simulation and Markov state models to explore the interactions between DHDPS from the human pathogen Staphylococcus aureus and its cognate substrate, pyruvate. Our simulations recover the crystallographic DHDPS-pyruvate complex without a priori knowledge of the final bound structure. The highly conserved residue Arg140 was found to have a pivotal role in coordinating the entry of pyruvate into the active site from bulk solvent, consistent with previous kinetic reports, indicating an indirect role for the residue in DHDPS catalysis. A metastable binding intermediate characterized by multiple points of intermolecular interaction between pyruvate and key DHDPS residue Arg140 was found to be a highly conserved feature of the binding trajectory when comparing alternative binding pathways. By means of umbrella sampling we show that these binding intermediates are thermodynamically metastable, consistent with both the available experimental data and the substrate binding model presented in this study. Our results provide insight into an important enzyme-substrate interaction in atomistic detail that offers the potential to be exploited for the discovery of more effective DHDPS inhibitors and, in a broader sense, dynamic protein-drug interactions.
Subject(s)
Hydro-Lyases/chemistry , Hydro-Lyases/ultrastructure , Models, Chemical , Molecular Dynamics Simulation , Pyruvic Acid/chemistry , Staphylococcus/enzymology , Binding Sites , Catalysis , Enzyme Activation , Enzyme Stability , Kinetics , Protein Binding , Protein Conformation , Substrate SpecificityABSTRACT
Here, we review recent studies aimed at defining the importance of quaternary structure to a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate the complementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugation with enzyme kinetics, in vitro mutagenesis, macromolecular crystallography, small angle X-ray scattering, and molecular dynamics simulations, to demonstrate the role of subunit self-association in facilitating protein dynamics and enzyme function. This multitechnique approach has yielded new insights into the molecular evolution of protein quaternary structure.
Subject(s)
Bacterial Proteins/chemistry , Hydro-Lyases/chemistry , Plant Proteins/chemistry , Bacterial Proteins/isolation & purification , Evolution, Molecular , Hydro-Lyases/isolation & purification , Kinetics , Molecular Dynamics Simulation , Plant Proteins/isolation & purification , Protein Multimerization , Protein Structure, Quaternary , Protein Subunits , Scattering, Small Angle , Ultracentrifugation , X-Ray DiffractionABSTRACT
The controlled dissolution of microdroplets on a supporting substrate is an effective approach that can be used to tune the assembled microstructure of basic units suspended within the droplet. In this work, we studied the self-assembly of two-dimensional graphene oxide (GO) nanosheets driven by the dissolution of a microdroplet situated at the interface between a solid substrate and the surrounding liquid phase. We found that although uniform microstructures form at the liquid-liquid interface of the droplets, the contact between the droplet and the substrate can give rise to a variety of different morphologies near the base of the droplet. In particular, pinning effects at the boundary of the dissolving droplet on the substrate lead to non-spherical GO assemblies. The results in this work demonstrate the possibility that tailored three-dimensional architectures of nanosheets assembled in a dissolving droplet may be achieved through control of the wetting properties of the droplet on the supporting substrate.
ABSTRACT
The malarial parasite Plasmodium falciparum is exposed to substantial redox challenges during its complex life cycle. In intraerythrocytic parasites, haemoglobin breakdown is a major source of reactive oxygen species. Deficiencies in human glucose-6-phosphate dehydrogenase, the initial enzyme in the pentose phosphate pathway (PPP), lead to a disturbed redox equilibrium in infected erythrocytes and partial protection against severe malaria. In P. falciparum, the first two reactions of the PPP are catalysed by the bifunctional enzyme glucose-6-phosphate dehydrogenase 6-phosphogluconolactonase (PfGluPho). This enzyme differs structurally from its human counterparts and represents a potential target for drugs. In the present study we used epitope tagging of endogenous PfGluPho to verify that the enzyme localises to the parasite cytosol. Furthermore, attempted double crossover disruption of the PfGluPho gene indicates that the enzyme is essential for the growth of blood stage parasites. As a further step towards targeting PfGluPho pharmacologically, ellagic acid was characterised as a potent PfGluPho inhibitor with an IC50 of 76 nM. Interestingly, pro-oxidative drugs or treatment of the parasites with H2O2 only slightly altered PfGluPho expression or activity under the conditions tested. Furthermore, metabolic profiling suggested that pro-oxidative drugs do not significantly perturb the abundance of PPP intermediates. These data indicate that PfGluPho is essential in asexual parasites, but that the oxidative arm of the PPP is not strongly regulated in response to oxidative challenge.
Subject(s)
Antimalarials/pharmacology , Carboxylic Ester Hydrolases/metabolism , Ellagic Acid/pharmacology , Glucosephosphate Dehydrogenase/metabolism , Multienzyme Complexes/metabolism , Plasmodium falciparum/drug effects , Antimalarials/chemistry , Blood/parasitology , Carboxylic Ester Hydrolases/antagonists & inhibitors , Cytosol/enzymology , Ellagic Acid/chemistry , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/pharmacology , Gene Knockout Techniques , Glucose/metabolism , Glucosephosphate Dehydrogenase/antagonists & inhibitors , Humans , Hydrogen Peroxide/pharmacology , Inhibitory Concentration 50 , Molecular Docking Simulation , Molecular Targeted Therapy , Multienzyme Complexes/antagonists & inhibitors , Oxidative Stress , Plasmodium falciparum/enzymology , Plasmodium falciparum/geneticsABSTRACT
Equinatoxin II (EqtII) is a soluble, 20 kDa pore-forming protein toxin isolated from the sea anemone Actinia equina. Although pore formation has long been known to occur in distinct stages, including monomeric attachment to phospholipid membranes followed by detachment of the N-terminal helical domain and oligomerization into the final pore assembly, atomistic-level detail of the protein-lipid interactions underlying these events remains elusive. Using high-resolution solution state NMR of uniformly-(15)N-labeled EqtII at the critical micelle concentration of dodecylphosphocholine, we have mapped the lipid-binding site through chemical shift perturbations. Subsequent docking of an EqtII monomer onto a dodecylphosphocholine micelle, followed by 400 ns of all-atom molecular dynamics simulation, saw several high-occupancy lipid-binding pockets stabilized by cation-π, hydrogen bonding, and hydrophobic interactions; and stabilization of the loop housing the conserved arginine-glycine-aspartate motif. Additional simulation of EqtII with an N-acetyl sphingomyelin micelle, for which high-resolution NMR data cannot be obtained due to aggregate formation, revealed that sphingomyelin specificity might occur via hydrogen bonding to the 3-OH and 2-NH groups unique to the ceramide backbone by side chains of D109 and Y113; and main chains of P81 and W112. Furthermore, a binding pocket formed by K30, K77, and P81, proximate to the hinge region of the N-terminal helix, was identified and may be implicated in triggering pore formation.
Subject(s)
Cnidarian Venoms/chemistry , Molecular Dynamics Simulation , Sphingomyelins/metabolism , Amino Acid Motifs , Amino Acid Sequence , Binding Sites , Cnidarian Venoms/metabolism , Magnetic Resonance Spectroscopy , Molecular Sequence Data , Phosphorylcholine/analogs & derivatives , Phosphorylcholine/chemistry , Phosphorylcholine/pharmacology , Protein Binding , Sphingomyelins/chemistryABSTRACT
The question of how many chains an elementary cellulose microfibril contains is critical to understanding the molecular mechanism(s) of cellulose biosynthesis and regulation. Given the hexagonal nature of the cellulose synthase rosette, it is assumed that the number of chains must be a multiple of six. We present molecular dynamics simulations on three different models of Iß cellulose microfibrils, 18, 24, and 36 chains, to investigate their structure and dynamics in a hydrated environment. The 36-chain model stays in a conformational space that is very similar to the initial crystalline phase, while the 18- and 24-chain models sample a conformational space different from the crystalline structure yet similar to conformations observed in recent high-temperature molecular dynamics simulations. Major differences in the conformations sampled between the different models result from changes to the tilt of chains in different layers, specifically a second stage of tilt, increased rotation about the O2-C2 dihedral, and a greater sampling of non-TG exocyclic conformations, particularly the GG conformation in center layers and GT conformation in solvent-exposed exocyclic groups. With a reinterpretation of nuclear magnetic resonance data, specifically for contributions made to the C6 peak, data from the simulations suggest that the 18- and 24-chain structures are more viable models for an elementary cellulose microfibril, which also correlates with recent scattering and diffraction experimental data. These data inform biochemical and molecular studies that must explain how a six-particle cellulose synthase complex rosette synthesizes microfibrils likely comprised of either 18 or 24 chains.
Subject(s)
Cellulose/chemistry , Molecular Dynamics Simulation , Cellobiose/chemistry , Dimerization , Hydrogen Bonding , Molecular Conformation , Polymerization , Water/chemistryABSTRACT
We study the effect of a neutral particle on the ionic flow through a nanopore using a basic uniform field theory and the coupled Poisson-Nernst-Planck and Navier-Stokes (PNP-NS) equations. We consider hourglass and cylindrical pore profiles and examine how the difference in pore shape changes the position dependence of the current change due to the particle. Good quantitative agreement between both calculations is seen, though we find that the simple theory is unable to correctly capture the change in the access resistance of the pore if a particle is placed at the pore entrance. Finally, we examine the spatial variations in the solutions of the PNP-NS equations, finding that the electro-osmotic flow through the pore is completely disrupted for sufficiently large particles.
ABSTRACT
Solid-state nanopores have been shown to be suitable for single molecule detection. While numerous modeling investigations exist for DNA within nanopores, there are few simulations of protein translocations. In this paper, we use atomistic molecular dynamics to investigate the translocation of proteins through a silicon nitride nanopore. The nanopore dimensions and profile are representative of experimental systems. We are able to calculate the change in blockade current and friction coefficient for different positions of the protein within the pore. The change in ionic current is found to be negligible until the protein is fully within the pore and the current is lowest when the protein is in the pore center. Using a simple theory that gives good quantitative agreement with the simulation results we are able to show that the variation in current with position is a function of the pore shape. In simulations that guide the protein through the nanopore we identify the effect that confinement has on the friction coefficient of the protein. This integrated view of translocation at the nanoscale provides useful insights that can be used to guide the design of future devices.
Subject(s)
Molecular Dynamics Simulation , Nanopores/ultrastructure , Streptavidin/analysis , Streptomyces/chemistry , Protein Transport , Streptavidin/metabolismABSTRACT
Diaminopimelate (DAP) epimerase is involved in the biosynthesis of meso-DAP and lysine, which are important precursors for the synthesis of peptidoglycan, housekeeping proteins, and virulence factors in bacteria. Accordingly, DAP epimerase is a promising antimicrobial target. Previous studies report that DAP epimerase exists as a monomeric enzyme. However, we show using analytical ultracentrifugation, X-ray crystallography, and enzyme kinetic analyses that DAP epimerase from Escherichia coli exists as a functional dimer in solution and the crystal state. Furthermore, the 2.0-Å X-ray crystal structure of the E. coli DAP epimerase dimer shows for the first time that the enzyme exists in an open, active conformation. The importance of dimerization was subsequently probed by using site-directed mutagenesis to generate a monomeric mutant (Y268A). Our studies show that Y268A is catalytically inactive, thus demonstrating that dimerization of DAP epimerase is essential for catalysis. Molecular dynamics simulations indicate that the DAP epimerase monomer is inherently more flexible than the dimer, suggesting that dimerization optimizes protein dynamics to support function. Our findings offer insight into the development of novel antimicrobial agents targeting the dimeric antibiotic target DAP epimerase.
Subject(s)
Amino Acid Isomerases/chemistry , Escherichia coli/enzymology , Anti-Bacterial Agents/chemistry , Catalytic Domain , Circular Dichroism , Crystallography, X-Ray/methods , Dimerization , Escherichia coli/metabolism , Lysine/chemistry , Models, Chemical , Models, Molecular , Molecular Conformation , Molecular Dynamics Simulation , Mutagenesis, Site-Directed , Mutation , Point Mutation , Protein Conformation , Protein Structure, SecondaryABSTRACT
Lysine is one of the most limiting amino acids in plants and its biosynthesis is carefully regulated through inhibition of the first committed step in the pathway catalyzed by dihydrodipicolinate synthase (DHDPS). This is mediated via a feedback mechanism involving the binding of lysine to the allosteric cleft of DHDPS. However, the precise allosteric mechanism is yet to be defined. We present a thorough enzyme kinetic and thermodynamic analysis of lysine inhibition of DHDPS from the common grapevine, Vitis vinifera (Vv). Our studies demonstrate that lysine binding is both tight (relative to bacterial DHDPS orthologs) and cooperative. The crystal structure of the enzyme bound to lysine (2.4 Å) identifies the allosteric binding site and clearly shows a conformational change of several residues within the allosteric and active sites. Molecular dynamics simulations comparing the lysine-bound (PDB ID 4HNN) and lysine free (PDB ID 3TUU) structures show that Tyr132, a key catalytic site residue, undergoes significant rotational motion upon lysine binding. This suggests proton relay through the catalytic triad is attenuated in the presence of lysine. Our study reveals for the first time the structural mechanism for allosteric inhibition of DHDPS from the common grapevine.
Subject(s)
Computational Biology , Hydro-Lyases/antagonists & inhibitors , Hydro-Lyases/chemistry , Lysine/pharmacology , Vitis/enzymology , Allosteric Regulation/drug effects , Allosteric Site , Bacteria/enzymology , Biosynthetic Pathways/drug effects , Calorimetry , Crystallography, X-Ray , Enzyme Stability/drug effects , Hydro-Lyases/metabolism , Kinetics , Lysine/biosynthesis , Molecular Dynamics Simulation , Protein Structure, Quaternary , Protein Structure, Secondary , Pyruvic Acid/metabolism , Solutions , Thermodynamics , Vitis/drug effectsABSTRACT
Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis in bacteria and plants. The structure of DHDPS has been determined from several bacterial species and shown in most cases to form a homotetramer or dimer of dimers. However, only one plant DHDPS structure has been determined to date from the wild tobacco species, Nicotiana sylvestris (Blickling et al. (1997) J. Mol. Biol. 274, 608-621). Whilst N. sylvestris DHDPS also forms a homotetramer, the plant enzyme adopts a 'back-to-back' dimer of dimers compared to the 'head-to-head' architecture observed for bacterial DHDPS tetramers. This raises the question of whether the alternative quaternary architecture observed for N. sylvestris DHDPS is common to all plant DHDPS enzymes. Here, we describe the structure of DHDPS from the grapevine plant, Vitis vinifera, and show using analytical ultracentrifugation, small-angle X-ray scattering and X-ray crystallography that V. vinifera DHDPS forms a 'back-to-back' homotetramer, consistent with N. sylvestris DHDPS. This study is the first to demonstrate using both crystal and solution state measurements that DHDPS from the grapevine plant adopts an alternative tetrameric architecture to the bacterial form, which is important for optimizing protein dynamics as suggested by molecular dynamics simulations reported in this study.
Subject(s)
Hydro-Lyases/chemistry , Recombinant Proteins/chemistry , Vitis/enzymology , Circular Dichroism , Cloning, Molecular , Computer Simulation , Crystallization , Crystallography, X-Ray , Hydro-Lyases/genetics , Hydro-Lyases/metabolism , Kinetics , Models, Molecular , Molecular Dynamics Simulation , Protein Multimerization , Protein Structure, Quaternary , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Scattering, Small Angle , SolutionsABSTRACT
We discuss the modelling of a microswimmer that operates in a 'squirmer' mode, by means of stochastic rotation dynamics. The squirmer that we model can easily be tuned between a 'pusher' and a 'puller'. We examine the flows produced by the squirmer and find that there is good agreement between both the predicted and simulated velocities of locomotion and the resulting flow field.
ABSTRACT
Kinetically constrained spin models are known to exhibit dynamical behavior mimicking that of glass forming systems. They are often understood as coarse-grained models of glass formers, in terms of some "mobility" field. The identity of this "mobility" field has remained elusive due to the lack of coarse-graining procedures to obtain these models from a more microscopic point of view. Here we exhibit a scheme to map the dynamics of a two-dimensional soft disk glass former onto a kinetically constrained spin model, providing an attempt at bridging these two approaches.