Biology subjects

Corey, R. A.

Publications and source records attributed to Corey, R. A..

At least 19 recordsLinked to original sources

bioRxiv2026

Identification and targeting of a novel drug pocket in the tumour angiogenesis regulator RhoJ

The Rho GTPase RhoJ is a key regulator of tumour angiogenesis and has been identified as a target for anti-angiogenic drug design. Its high sequence conservation with the related Rho GTPase Cdc42 complicates selective drug discovery. RhoJ has a unique N-terminal extension (Asn2-Lys19) that is absent in Cdc42 and other Rho GTPases. Here, we use molecular dynamics simulations to identify a novel allosteric pocket formed by the RhoJ N-terminus and show that this pocket contributes to interactions with key downstream signalling partners. Structure-based virtual screening of small molecules targeting this pocket identified the antifungal terconazole as a potential binder. Computational docking revealed that terconazole occupies the N-terminal pocket, sharing critical contacts with the interface between RhoJ and PAK3, a key interacting partner. To validate this, we developed an optimized bioluminescence resonance energy transfer (eBRET2)-based biosensor to monitor the interaction between RhoJ and PAK3 in live cells and saw that terconazole disrupted the RhoJ:PAK3 interaction in a dose-dependent manner. Together, our MD results show that the RhoJ N-terminal extension assumes structure on binding to PAK3 and contributes to that interaction, while our cellular biosensor data support targeting this pocket to modulate the RhoJ:PAK3 interaction. The ability of terconazole to bind to the N-terminal pocket and disrupt PAK3 binding provides proof of concept for the specific targeting of RhoJ in the development of novel anti-angiogenic drugs.

biochemistry↗

bioRxiv2026

Benchmarking AI-generated structural ensembles of membrane proteins against physics-based modelling

Proteins dynamically switch between a continuum of interconverting conformational states, and understanding these structural dynamics is important for understanding protein function and for developing therapeutics. Molecular dynamics (MD) simulations can provide insight into protein conformational ensembles, but sampling rare conformational states can require substantial computational resources. The recent development of AI-based approaches for generating protein conformational ensembles, such as the Biomolecular Emulator (BioEmu), offers a potential alternative, although it remains unclear whether these approaches can accurately capture the conformational landscapes, especially for special cases such as membrane proteins. Here, we assess the ability of BioEmu to model the conformational dynamics of a model membrane protein, the bacterial rhomboid intramembrane proteases GlpG. We find that BioEmu generates a range of conformations corresponding to both open and closed states of the rhomboid lateral gate, including states associated with different stages of the catalytic cycle. These conformations broadly correspond to states sampled during microsecond-timescale MD simulations, although BioEmu does not reproduce the full conformational landscape observed using MD. BioEmu also samples substantial conformational heterogeneity within the soluble domains of rhomboids, which are highly flexible and poorly represented in experimental structures. Overall, our findings demonstrate that BioEmu can generate plausible conformational ensembles for relatively large, six-and seven-pass membrane proteins, sampling rare states at a fraction of the computational cost of conventional MD simulations. These results suggest that AI-based ensemble generation could provide an accessible approach for exploring membrane protein dynamics and complement conventional molecular modelling approaches.

biophysics↗

bioRxiv2026

Integrating AI and molecular modeling for structural prediction of a closed state of the hERG channel

The voltage-gated potassium channel hERG (Kv11.1) plays a central role in cardiac repolarisation by mediating the rapid delayed rectifier K+ current (IKr). Blockage of hERG by small molecules can lead to delayed repolarisation, QT interval prolongation, and potentially fatal arrhythmias, making the channel a critical focus in drug safety screening. Despite extensive pharmacological and electrophysiological characterisation, a complete structural understanding of hERG gating remains limited by the absence of an experimentally determined closed-state structure. Here, we use AI-based structural modelling to predict and compare candidate closed conformations of hERG. Building on recent work in which AlphaFold2 (AF2) predictions guided by engineered structural templates captured closed and inactivated states, we applied the emerging protein structure predictor, Chai-1, which employs a single-sequence, language model-based approach independent of multiple-sequence alignments. The resulting Chai-1 hERG model was compared with the AF2-derived closed structure, a homology model based on the Rattus norvegicus EAG channel, and an experimentally resolved open-state cryo-EM structure. We assessed these models using a combination of all-atom and coarse-grained molecular dynamics simulations, analysing protein dynamics, pore geometry, gating residue orientation, hydration, and lipid interactions. The Chai-1 and AF2 models displayed strong structural and dynamic agreement, both adopting compact, non-conductive conformations consistent with a physiologically closed state. Our data reveal insights into VSD dynamics, as well as suggesting a state dependence for ceramide binding at the previously identified M651 residue. Our findings support the validity of AI-derived closed-state hERG models and underscore the growing potential of deep learning-based protein structure prediction to identify previously uncharacterised, pharmacologically relevant conformations of membrane proteins. Further, our Chai-1 derived closed state model expands our structural insights into hERG gating and may have utility for investigation of drug-hERG interactions.

biochemistry↗

bioRxiv2025

Structural and energetic insights into human rhomboid proteases reveal a unique lateral gating mechanism for orphan family members

Rhomboid proteases play fundamental roles in human biology and disease by cleaving substrate transmembrane domains. However, the absence of structural data and the inability to identify substrates for orphan human rhomboids limit mechanistic understanding. Lateral gating is considered the primary route by which transmembrane substrates access the rhomboid active site, although this has been demonstrated directly only for the bacterial rhomboid GlpG. To address this, we characterised the structures, conformational ensembles, and energy landscapes of human rhomboid proteases using AI-based structural models and molecular dynamics simulations, benchmarked by simulations seeded with GlpG crystal structures and models. We find that while some human rhomboids readily transition to open conformations compatible with transmembrane substrate access, orphan rhomboids possess unusually narrow lateral gates that require substantially higher energy to open. Our results reveal unexpected diversity in substrate engagement mechanisms among human rhomboids, and provide a rationale for the orphan status of recently evolved family members.

biochemistry↗

bioRxiv2025

The growth-promoting protein TMEM263 is an ER resident that controls early stages of lipid droplet biogenesis

Cell and organismal growth is controlled not only by the availability of nutrients, but also the ability to dynamically sense and respond to changes in metabolic demand. We have identified a protein, TMEM263 (also known as C12orf23) as a new mechanistic link between growth and lipid metabolism. TMEM263 was discovered in a screen as an ER-resident protein, and we have characterised its role as both necessary and sufficient for lipid droplet formation. TMEM263 has two transmembrane domains that fold into a hairpin structure which are essential for its localisation to the ER and to lipid droplets. Functionally, we propose that TMEM263 can interact with and support the condensation of neutral lipids in a bilayer to promote lipid droplet formation and growth. Consistently, loss of TMEM263 in cells and in zebrafish significantly impairs lipid droplet formation. Loss of TMEM263 protein function in vivo is associated with organismal growth defects and proportional dwarfism and our study provides a mechanistic understanding linking these phenotypes to impaired lipid droplet biology.

cell biology↗

bioRxiv2025

Insights from aquaporin structures into drug-resistant sleeping sickness

Trypanosoma brucei is the causal agent of African trypanosomiasis in humans and animals, the latter resulting in significant negative economic impacts in afflicted areas of the world. Resistance has arisen to the trypanocidal drugs pentamidine and melarsoprol through mutations in the aquaglyceroporin TbAQP2 that prevent their uptake. Here we use cryogenic electron microscopy to determine the structure of TbAQP2 from Trypanosoma brucei, bound to either the substrate glycerol or to the sleeping sickness drugs, pentamidine or melarsoprol. The drugs bind within the AQP2 channel at a site completely overlapping that of glycerol. Mutations leading to a drug-resistant phenotype were found in the channel lining. Molecular dynamics simulations showed the channel can be traversed by pentamidine, with a low energy binding site at the centre of the channel, flanked by regions of high energy association at the extracellular and intracellular ends. Drug-resistant TbAQP2 mutants are still predicted to bind pentamidine, but the much weaker binding in the centre of the channel observed in the MD simulations would be insufficient to compensate for the high energy processes of ingress and egress, hence impairing transport at pharmacologically relevant concentrations. The structures of drug-bound TbAQP2 represent a novel paradigm for drug-transporter interactions that could provide new mechanisms for targeting drugs into pathogens and human cells.

molecular biology↗

bioRxiv2024

The Role of Cholesterol in M2 Clustering and Viral Budding Explained

The proton-conducting domain of the influenza A M2 homotetrameric channel (M2TM-AH; residues 22-62), consisting of four transmembrane (TM; residues 22-46) and four amphipathic helices (AHs; residues 47-62), promotes the release of viral RNA via acidification. Previous studies have also proposed the formation of clusters of M2 channels in the budding neck areas in raft-like domains of the plasma membrane, 1,2 which are rich in cholesterol, resulting in cell membrane scission and viral release. Experiments showed that cholesterol has a significant contribution to lipid bilayer undulations in viral buds suggesting a significant role for cholesterol in the budding process. However, a clear explanation of membrane curvature effect based on the distribution of cholesterol around M2TM-AH clusters is lacking. Using coarse-grained molecular dynamics simulations of M2TM-AH in bilayers, we observed that M2 channels form specific clusters with conical shapes, driven by attraction of their amphipathic helices (AHs). We showed that cholesterol stabilized the formation of M2 channel clusters, by filling and bridging the conical gap between M2 channels at specific sites in the N-terminals of adjacent channels or via the C-terminal region of TM and AHs, the latter sites displaying longer interaction time and higher stability. Potential of mean force calculations showed that when cholesterols occupy the identified interfacial binding sites between two M2 channels, the dimer is stabilized by 11 kJ/mol. This translates to the cholesterol-bound dimer being populated by almost two orders of magnitude compared to a dimer lacking cholesterol. We demonstrated that the cholesterol bridged M2 channels can exert lateral force on the surrounding membrane to induce the necessary negative Gaussian curvature profile which permits the spontaneous scission of the catenoid membrane neck and leads to viral buds and scission. Significance StatementA key role of influenza A M2 channel, a prototype viroporin, is the generation of curvature in the host cell membrane to form budding necks leading to scission and release of the virions. It has been shown experimentally that this process is mediated through the amphipathic helices of M2 and that cholesterol enhanced lipid bilayer undulations in viral budding. Here, using coarse-grained molecular dynamics simulations we revealed that M2 channels form clusters in membranes, induced in an additive manner by both the AHs and cholesterol, which in turn increase local membrane curvature. We showed that both cluster formation and the induced membrane curvature are enhanced by cholesterol by bridging the conical area between M2 channels.

biophysics↗

bioRxiv2024

Engineering cardiolipin binding to an artificial membrane protein

Integral membrane proteins carry out essential functions in the cell, and their activities are often modulated by specific protein-lipid interactions in the membrane. Here, we elucidate the intricate role of cardiolipin (CDL), a regulatory lipid, as a stabilizer of membrane proteins and their complexes. Using the in silico-designed model protein TMHC4_R (ROCKET) as a scaffold, we employ a combination of molecular dynamics simulations and native mass spectrometry to explore the protein features that facilitate preferential lipid interactions and mediate stabilization. We find that the spatial arrangement of positively charged residues as well as local conformational flexibility are factors that distinguish stabilizing from non-stabilizing CDL interactions. However, we also find that even in this controlled, artificial system, a clear-cut distinction between binding and stabilization is difficult to attain, revealing that overlapping lipid contacts can partially compensate for the effects of binding site mutations. Extending our insights to naturally occurring proteins, we identify a stabilizing CDL site within the E. coli rhomboid intramembrane protease GlpG and uncover its regulatory influence on enzyme substrate preference. In this work, we establish a framework for engineering functional lipid interactions, paving the way for the design of proteins with membrane-specific properties or functions.

biochemistry↗

bioRxiv2024

Coarse-graining the recognition of a glycolipid by the C-type lectin Mincle receptor

Macrophage inducible Ca2+-dependent lectin (Mincle) receptor recognizes Mycobacterium tuberculosis glycolipids to trigger an immune response. This host membrane receptor is thus a key player in the modulation of the immune response to infection by M. tuberculosis, and has emerged as a promising target for the development of new vaccines for tuberculosis. The recent development of the Martini 3 force field for coarse-grained (CG) molecular modeling allow the study of interactions of soluble proteins with small ligands but its use for the study of interactions with lipids remains less explored. Here, we present a refined approach detailing a protocol for modeling such interactions at a CG level using the Martini 3 force field. Using this approach, we studied Mincle and identified critical parameters governing ligand recognition, such as loop flexibility and the regulation of hydrophobic groove formation by calcium ions. In addition, we assessed ligand affinity using free energy perturbation calculations. Our results offer mechanistic insight into the interactions between Mincle and glycolipids, providing a basis for rational design of molecules targeting this type of membrane receptors.

bioinformatics↗

bioRxiv2023

A feedback control mechanism governs the synthesis of lipid-linked precursors of the bacterial cell wall

Many bacterial surface glycans such as the peptidoglycan (PG) cell wall, O-antigens, and capsules are built from monomeric units linked to a polyprenyl lipid carrier. How this limiting lipid carrier is effectively distributed among competing pathways has remained unclear for some time. Here, we describe the isolation and characterization of hyperactive variants of Pseudomonas aeruginosa MraY, the essential and conserved enzyme catalyzing the formation of the first lipid-linked PG precursor called lipid I. These variants result in the elevated production of the final PG precursor lipid II in cells and are hyperactive in a purified system. Amino acid substitutions within the activated MraY variants unexpectedly map to a cavity on the extracellular side of the dimer interface, far from the active site. Our structural evidence and molecular dynamics simulations suggest that the cavity is a binding site for lipid II molecules that have been transported to the outer leaflet of the membrane. Overall, our results support a model in which excess externalized lipid II allosterically inhibits MraY, providing a feedback mechanism to prevent the sequestration of lipid carrier in the PG biogenesis pathway. MraY belongs to the broadly distributed polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase (PNPT) superfamily of enzymes. We therefore propose that similar feedback mechanisms may be widely employed to coordinate precursor supply with demand by polymerases, thereby optimizing the partitioning of lipid carriers between competing glycan biogenesis pathways.

microbiology↗

bioRxiv2023

The Energetics and Ion Coupling of Cholesterol Transport Through Patched1

Patched1 (PTCH1) is the principal tumour suppressor protein of the mammalian Hedgehog (HH) signalling pathway, implicated in embryogenesis and tissue homeostasis. PTCH1 inhibits the Class F G protein-coupled receptor Smoothened (SMO) via a debated mechanism involving modulating accessible cholesterol levels within ciliary membranes. Using extensive molecular dynamics (MD) simulations and free energy calculations to evaluate cholesterol transport through PTCH1, we find an energetic barrier of ~15-20 kJ mol-1 for cholesterol export. In simulations we identify cation binding sites within the PTCH1 transmembrane domain (TMD) which may provide the energetic impetus for cholesterol transport. In silico data are coupled to in vivo biochemical assays of PTCH1 mutants to probe coupling between transmembrane motions and PTCH1 activity. Using complementary simulations of Dispatched1 (DISP1) we find that transition between inward-open and solvent occluded states is accompanied by Na+ induced pinching of intracellular helical segments. Thus, our findings illuminate the energetics and ion-coupling stoichiometries of PTCH1 transport mechanisms, whereby 1-3 Na+ or 2-3 K+ couple to cholesterol export, and provide the first molecular description of transitions between distinct transport states.

biophysics↗

bioRxiv2023

Cyclic di-AMP traps proton-coupled K+ transporters of the KUP 1 family in an inward-occluded conformation

Cyclic di-AMP is the only known essential second messenger in bacteria and archaea, regulating different proteins indispensable for numerous physiological processes. In particular, it controls various potassium and osmolyte transporters involved in osmoregulation. In Bacillus subtilis, the K+/H+ symporter KimA of the KUP family is inactivated by c-di-AMP. KimA sustains survival at potassium limitation at low external pH by mediating K+ ions uptake. However, at elevated intracellular K+ concentrations, further K+ accumulation would be toxic. In this study, we reveal the molecular basis of how c-di-AMP binding inhibits KimA. We report cryo-EM structures of KimA with bound c-di-AMP in detergent solution and reconstituted in amphipols. By combining structural data with functional assays and molecular dynamics simulations we reveal how c-di-AMP modulates transport. We show that an intracellular loop in the transmembrane domain interacts with c-di-AMP bound to the adjacent cytosolic domain. This reduces the mobility of transmembrane helices at the cytosolic side of the K+ binding site and therefore traps KimA in an inward-occluded conformation.

biophysics↗

bioRxiv2022

Comparative Study of State-Dependent Cholesterol Binding Sites in Adenosine A2A and A1 Receptors Using Coarse-Grained Molecular Dynamics Simulations in Biologically Relevant Membranes

In this study we used coarse-grained molecular dynamics (CG MD) simulations to study protein-cholesterol interactions for different activation states of the A2A adenosine receptor (A2AR) and A1 adenosine receptor (A1R). Three different membranes were used, of which a plasma mimetic membrane best matched cholesterol binding sites previously detected in X-ray structures and computationally for the inactive state of A2AR. Here, cholesterol binds stably between TM5 and TM6 in the intracellular leaf and between the extracellular part of TM6 and TM7. The stability of the identified binding sites to A1R with CG MD simulations were further investigated using potential of mean force calculations combined with umbrella sampling. Cholesterol binding to certain cavities in active or inactive state can stabilize a conformation of active or inactive state respectively and is important to identify these cavities. For the active state the cholesterol binding sites have much longer residence times compared to the inactive state for both A2AR and A1R. We observed for the active A1R two cholesterol binding sites in the extracellular membrane leaf in a cavity between TM2/TM3 and along TM3 in the intracellular leaf. We found a partially overlapped binding area between TM6 and TM7 in the extracellular membrane leaf for active state and inactive A1R state which can be antagonized by cholesterol molecules although the site has a much longer residence time for active A1R. For the active A2AR we predicted a high residence time cholesterol position between TM1 and TM7 in the middle region of TMD which is different from the binding sites calculated in active or inactive A1R and for the inactive A2AR. For the inactive A2AR cholesterol binds to the same extracellular area between TM6 and TM7 as in the inactive A1R. The differences in stable, long residence time cholesterol binding sites between active and inactive states of A1R and for A2AR can be important for functional activity and orthosteric agonist or antagonist affinity and can be used for the design of allosteric modulators which can bind through lipid pathways.

biophysics↗

bioRxiv2022

Cardiolipin, and not monolysocardiolipin, preferentially binds to the interface of Complexes III and IV

The mitochondrial electron transport chain comprises a series of protein complexes embedded in the inner mitochondrial membrane that generate a proton motive force via oxidative phosphorylation, ultimately generating ATP. These protein complexes can oligomerize to form larger structures called supercomplexes. Cardiolipin (CL), a conical lipid, unique within eukaryotes to the inner mitochondrial membrane, has proven essential in maintaining the stability and function of supercomplexes. Monolysocardiolipin (MLCL) is a CL variant that accumulates in people with Barth syndrome (BTHS). BTHS is caused by defects in CL biosynthesis and characterised by abnormal mitochondrial bioenergetics and destabilised supercomplexes. However, the mechanisms by which MLCL causes pathogenesis remain unclear. Here, multiscale molecular dynamics characterise the interactions of CL and MLCL with yeast and mammalian mitochondrial supercomplexes containing Complex III (CIII) and Complex IV (CIV). Coarse-grained simulations reveal that both CL and MLCL bind to sites at the interface between CIII and CIV of the supercomplex. Free energy perturbation calculations show that MLCL interaction is weaker than that of CL and suggest that interaction with CIV drives this difference. Atomistic contact analyses show that, although interaction with CIII is similar for CL and MLCL, CIV makes more contacts with CL than MLCL, demonstrating that CL is a more successful "glue" between the two complexes. Simulations of the human CIII2CIV supercomplex show that this interface site is maintained between species. Our study suggests that MLCL accumulation in people with BTHS disrupts supercomplex stability by formation of relatively weak interactions at the interface lipid binding site.

biochemistry↗

bioRxiv2022

LipIDens: Simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins.

Cryo-electron microscopy (cryo-EM) enables the determination of membrane protein structures in native-like environments. Characterising how membrane proteins interact with the surrounding membrane lipid environment is assisted by resolution of lipid-like densities visible in cryo-EM maps. Nevertheless, establishing the molecular identity of putative lipid and/or detergent densities remains challenging. Here we present LipIDens, a pipeline for molecular dynamics (MD) simulation-assisted interpretation of lipid and lipid-like densities in cryo-EM structures. The pipeline integrates the implementation and analysis of multi-scale MD simulations for identification, ranking and refinement of lipid binding poses which superpose onto cryo-EM map densities. Thus, LipIDens enables direct integration of experimental and computational structural approaches to facilitate the interpretation of lipid-like cryo-EM densities and to reveal the molecular identities of protein-lipid interactions within a bilayer environment. The LipIDens code is open-source and embedded within a notebook format to assist automation and usability.

biophysics↗

bioRxiv2022

From Molecular Dynamics to Supramolecular Organization: The Role of PIM Lipids in the Originality of the Mycobacterial Plasma Membrane

Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis, a disease that claims ~1.5 million lives annually. The current treatment regime is long and expensive, and missed doses contribute to drug resistance. There is much to be understood about the Mtb cell envelope, a complicated barrier that antibiotics need to negotiate to enter the cell. Within this envelope, the plasma membrane is the ultimate obstacle and is proposed to be comprised of over 50% mannosylated phosphatidylinositol lipids (phosphatidyl-myoinositol mannosides, PIMs), whose role in the membrane structure remains elusive. Here we used multiscale molecular dynamics (MD) simulations to understand the structure-function relationship of the PIM lipid family and decipher how they self-organize to drive biophysical properties of the Mycobacterial plasma membrane. To validate the model, we tested known anti-tubercular drugs and replicated previous experimental results. Our results shed new light into the organization of the Mycobacterial plasma membrane and provides a working model of this complex membrane to use for in silico studies. This opens the door for new methods to probe potential antibiotic targets and further understand membrane protein function. O_FIG O_LINKSMALLFIG WIDTH=169 HEIGHT=200 SRC="FIGDIR/small/498153v1_ufig1.gif" ALT="Figure 1"> View larger version (56K): org.highwire.dtl.DTLVardef@102b357org.highwire.dtl.DTLVardef@4c30f8org.highwire.dtl.DTLVardef@22f32aorg.highwire.dtl.DTLVardef@8a6f65_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗

bioRxiv2022

Inhibited KdpFABC resides in an E1 off-cycle state

KdpFABC is a high-affinity prokaryotic K+ uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K+ levels, KdpFABC needs to be inhibited to prevent excessive K+ accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES162 motif in the A domain of the pump subunit KdpB (KdpBS162-P). Here, we explore the structural basis of inhibition by KdpBS162 phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC conformation that we termed E1-P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1-P state adopted by KdpFABC upon KdpBS162 phosphorylation. The E1-P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1-P states to E2-P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such conformations.

molecular biology↗

bioRxiv2021

PyLipID: A Python package for analysis of protein-lipid interactions from MD simulations

Lipids play important modulatory and structural roles for membrane proteins. Molecular dynamics simulations are frequently used to provide insights into the nature of these proteinlipid interactions. Systematic comparative analysis requires tools that provide algorithms for objective assessment of such interactions. We introduce PyLipID, a python package for the identification and characterization of specific lipid interactions and binding sites on membrane proteins from molecular dynamics simulations. PyLipID uses a community analysis approach for binding site detection, calculating lipid residence times for both the individual protein residues and the detected binding sites. To assist structural analysis, PyLipID produces representative bound lipid poses from simulation data, using a density-based scoring function. To estimate residue contacts robustly, PyLipID uses a dual-cutoff scheme to differentiate between lipid conformational rearrangements whilst bound from full dissociation events. In addition to the characterization of protein-lipid interactions, PyLipID is applicable to analysis of the interactions of membrane proteins with other ligands. By combining automated analysis, efficient algorithms, and open-source distribution, PyLipID facilitates the systematic analysis of lipid interactions from large simulation datasets of multiple species of membrane proteins. ToC Graphic O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=143 SRC="FIGDIR/small/452312v1_ufig1.gif" ALT="Figure 1"> View larger version (53K): org.highwire.dtl.DTLVardef@1f6530corg.highwire.dtl.DTLVardef@c639d5org.highwire.dtl.DTLVardef@1fef967org.highwire.dtl.DTLVardef@a80446_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗