Bibliographies thématiques / Mechanics and kinetics of myosin motors

Littérature scientifique sur le sujet « Mechanics and kinetics of myosin motors »

Auteur : Grafiati

Publié le 10 mars 2023

Créez une référence correcte selon les styles APA, MLA, Chicago, Harvard et plusieurs autres

Choisissez une source :

Consultez les listes thématiques d’articles de revues, de livres, de thèses, de rapports de conférences et d’autres sources académiques sur le sujet « Mechanics and kinetics of myosin motors ».

À côté de chaque source dans la liste de références il y a un bouton « Ajouter à la bibliographie ». Cliquez sur ce bouton, et nous générerons automatiquement la référence bibliographique pour la source choisie selon votre style de citation préféré : APA, MLA, Harvard, Vancouver, Chicago, etc.

Vous pouvez aussi télécharger le texte intégral de la publication scolaire au format pdf et consulter son résumé en ligne lorsque ces informations sont inclues dans les métadonnées.

Articles de revues sur le sujet "Mechanics and kinetics of myosin motors"

Nayak, Arnab, Tianbang Wang, Peter Franz, Walter Steffen, Igor Chizhov, Georgios Tsiavaliaris et Mamta Amrute-Nayak. « Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function ». Journal of Biological Chemistry 295, n^o 20 (9 avril 2020) : 7046–59. http://dx.doi.org/10.1074/jbc.ra120.012774.

Texte intégral

Résumé :

Myosin II is the main force-generating motor during muscle contraction. Myosin II exists as different isoforms that are involved in diverse physiological functions. One outstanding question is whether the myosin heavy chain (MHC) isoforms alone account for these distinct physiological properties. Unique sets of essential and regulatory light chains (RLCs) are known to assemble with specific MHCs, raising the intriguing possibility that light chains contribute to specialized myosin functions. Here, we asked whether different RLCs contribute to this functional diversification. To this end, we generated chimeric motors by reconstituting the MHC fast isoform (MyHC-IId) and slow isoform (MHC-I) with different light-chain variants. As a result of the RLC swapping, actin filament sliding velocity increased by ∼10-fold for the slow myosin and decreased by >3-fold for the fast myosin. Results from ensemble molecule solution kinetics and single-molecule optical trapping measurements provided in-depth insights into altered chemo-mechanical properties of the myosin motors that affect the sliding speed. Notably, we found that the mechanical output of both slow and fast myosins is sensitive to the RLC isoform. We therefore propose that RLCs are crucial for fine-tuning the myosin function.

Styles APA, Harvard, Vancouver, ISO, etc.

Greenberg, Michael J., Tianming Lin, Henry Shuman et E. Michael Ostap. « Mechanochemical tuning of myosin-I by the N-terminal region ». Proceedings of the National Academy of Sciences 112, n^o 26 (8 juin 2015) : E3337—E3344. http://dx.doi.org/10.1073/pnas.1506633112.

Texte intégral

Résumé :

Myosins are molecular motors that generate force to power a wide array of motile cellular functions. Myosins have the inherent ability to change their ATPase kinetics and force-generating properties when they encounter mechanical loads; however, little is known about the structural elements in myosin responsible for force sensing. Recent structural and biophysical studies have shown that myosin-I isoforms, Myosin-Ib (Myo1b) and Myosin-Ic (Myo1c), have similar unloaded kinetics and sequences but substantially different responses to forces that resist their working strokes. Myo1b has the properties of a tension-sensing anchor, slowing its actin-detachment kinetics by two orders of magnitude with just 1 pN of resisting force, whereas Myo1c has the properties of a slow transporter, generating power without slowing under 1-pN loads that would stall Myo1b. To examine the structural elements that lead to differences in force sensing, we used single-molecule and ensemble kinetic techniques to show that the myosin-I N-terminal region (NTR) plays a critical role in tuning myosin-I mechanochemistry. We found that replacing the Myo1c NTR with the Myo1b NTR changes the identity of the primary force-sensitive transition of Myo1c, resulting in sensitivity to forces of <2 pN. Additionally, we found that the NTR plays an important role in stabilizing the post–power-stroke conformation. These results identify the NTR as an important structural element in myosin force sensing and suggest a mechanism for generating diversity of function among myosin isoforms.

Styles APA, Harvard, Vancouver, ISO, etc.

Littlefield, Kimberly Palmiter, Douglas M. Swank, Becky M. Sanchez, Aileen F. Knowles, David M. Warshaw et Sanford I. Bernstein. « The converter domain modulates kinetic properties ofDrosophila myosin ». American Journal of Physiology-Cell Physiology 284, n^o 4 (1 avril 2003) : C1031—C1038. http://dx.doi.org/10.1152/ajpcell.00474.2002.

Texte intégral

Résumé :

Recently the converter domain, an integral part of the “mechanical element” common to all molecular motors, was proposed to modulate the kinetic properties of Drosophila chimeric myosin isoforms. Here we investigated the molecular basis of actin filament velocity ( V actin) changes previously observed with the chimeric EMB-IC and IFI-EC myosin proteins [the embryonic body wall muscle (EMB) and indirect flight muscle isoforms (IFI) with genetic substitution of the IFI and EMB converter domains, respectively]. In the laser trap assay the IFI and IFI-EC myosins generate the same unitary step displacement (IFI = 7.3 ± 1.0 nm, IFI-EC = 5.8 ± 0.9 nm; means ± SE). Thus converter-mediated differences in the kinetics of strong actin-myosin binding, rather than the mechanical capabilities of the protein, must account for the observed V actin values. Basal and actin-activated ATPase assays and skinned fiber mechanical experiments definitively support a role for the converter domain in modulating the kinetic properties of the myosin protein. We propose that the converter domain kinetically couples the Pi and ADP release steps that occur during the cross-bridge cycle.

Styles APA, Harvard, Vancouver, ISO, etc.

Lecarpentier, Edouard R., Victor A. Claes, Oumar Timbely, Abdelilah Arsalane, Jacques A. Wipff, Jean-Louis M. Hébert, Francine Y. Michel et Yves C. Lecarpentier. « Mechanics and energetics of myosin molecular motors from nonpregnant human myometrium ». Journal of Applied Physiology 111, n^o 4 (octobre 2011) : 1096–105. http://dx.doi.org/10.1152/japplphysiol.00414.2011.

Texte intégral

Résumé :

Mechanical properties of spontaneously contracting isolated nonpregnant human myometrium (NPHM) were investigated throughout the whole continuum of load from zero load up to isometry. This made it possible to assess the three-dimensional tension-velocity-length (T-V-L) relationship characterizing the level of contractility and to determine crossbridge (CB) kinetics of myosin molecular motors. Seventy-seven muscle strips were obtained from hysterectomy in 42 nonpregnant patients. Contraction and relaxation parameters were measured during spontaneous mechanical activity. The isotonic tension-peak velocity (T-V) relationship was hyperbolic in 30 cases and nonhyperbolic in 47 cases. When the T-V relationship was hyperbolic, the Huxley formalism could be used to calculate CB kinetics and CB unitary force. At the whole muscle level and for a given isotonic load level, part of the V-L phase plane showed a common pathway, so that a given instantaneous length corresponded to only one possible instantaneous velocity, independent of time and initial length. At the molecular level, rate constants for CB attachment and detachment were dramatically low, ∼100 times lower than those of striated muscles, and ∼5 to 10 times lower than those of other smooth muscles. The CB unitary force was ∼1.4 ± 0.1 pN. NPHM shared similar basic contractile properties with striated muscles, reflected in the three-dimensional T-V-L relationship characterizing the contractile level. Low CB attachment and detachment rate constants made it possible to generate normal CB unitary force and normal muscle tension in NPHM, even though it contracted extremely slowly compared with other muscles.

Styles APA, Harvard, Vancouver, ISO, etc.

Marcucci, Lorenzo, Hiroki Fukunaga, Toshio Yanagida et Mitsuhiro Iwaki. « The Synergic Role of Actomyosin Architecture and Biased Detachment in Muscle Energetics : Insights in Cross Bridge Mechanism beyond the Lever-Arm Swing ». International Journal of Molecular Sciences 22, n^o 13 (29 juin 2021) : 7037. http://dx.doi.org/10.3390/ijms22137037.

Texte intégral

Résumé :

Muscle energetics reflects the ability of myosin motors to convert chemical energy into mechanical energy. How this process takes place remains one of the most elusive questions in the field. Here, we combined experimental measurements of in vitro sliding velocity based on DNA-origami built filaments carrying myosins with different lever arm length and Monte Carlo simulations based on a model which accounts for three basic components: (i) the geometrical hindrance, (ii) the mechano-sensing mechanism, and (iii) the biased kinetics for stretched or compressed motors. The model simulations showed that the geometrical hindrance due to acto-myosin spatial mismatching and the preferential detachment of compressed motors are synergic in generating the rapid increase in the ATP-ase rate from isometric to moderate velocities of contraction, thus acting as an energy-conservation strategy in muscle contraction. The velocity measurements on a DNA-origami filament that preserves the motors’ distribution showed that geometrical hindrance and biased detachment generate a non-zero sliding velocity even without rotation of the myosin lever-arm, which is widely recognized as the basic event in muscle contraction. Because biased detachment is a mechanism for the rectification of thermal fluctuations, in the Brownian-ratchet framework, we predict that it requires a non-negligible amount of energy to preserve the second law of thermodynamics. Taken together, our theoretical and experimental results elucidate less considered components in the chemo-mechanical energy transduction in muscle.

Styles APA, Harvard, Vancouver, ISO, etc.

Vargiu, Romina, Anna Perinu, Antonello De Lisa, Frank Tintrup, Francesco Manca et Rino Mancinelli. « Origin of Motion in the Human Ureter : Mechanics, Energetics and Kinetics of the Myosin Molecular Motors ». Urologia Journal 79, n^o 2 (avril 2012) : 123–29. http://dx.doi.org/10.5301/ru.2012.9110.

Texte intégral

Résumé :

Background Ureteral peristalsis is the result of coordinated mechanical motor performance of longitudinal and circular smooth muscle layer of the ureter wall. The main aim of this study was to characterize in smooth muscle of proximal segments of human ureter, the mechanical properties at level of muscle tissue and at level of myosin molecular motors. Methods Ureteral samples were collected from 15 patients, who underwent nephrectomy for renal cancer. Smooth muscle strips longitudinally and circularly oriented from proximal segments of human ureter were used for the in vitro experiments. Mechanical indices including the maximum unloaded shortening velocity (Vmax), and the maximum isometric tension (P0) normalized per cross-sectional area, were determined in vitro determined in electrically evoked contractions of longitudinal and circular smooth muscle strips. Myosin cross-bridge (CB) number per mm2 (Ψ) the elementary force per single CB (Ψ) and kinetic parameters were calculated in muscle strips, using Huxley's equations adapted to nonsarcomeric muscles. Results Longitudinal smooth muscle strips exhibited a significantly (p<0.05) faster Vmax (63%) and a higher P0 (40%), if compared to circular strips. Moreover, longitudinal muscle strips showed a significantly higher unitary force (Ψ) per CB. However, no significant differences were observed in CB number, the attachment (f1) and the detachment (g2) rate constants between longitudinal and circular muscle strips. Conclusions The main result obtained in the present work documents that the mechanical, energetic and unitary forces per CB of longitudinal layer of proximal ureter are better compared to the circular one; these preliminary findings suggested, unlike intestinal smooth muscle, a major role of longitudinal smooth muscle layer in the ureter peristalsis.

Styles APA, Harvard, Vancouver, ISO, etc.

Lecarpentier, Yves. « Mechanical and Thermodynamic Properties of Mesenchymal Stem Cells Differentiated into Myofibroblasts : A Commentary on the Article “Statistical Mechanics of Non-Muscle Myosin IIA in Human Bone Marrow-Derived Mesenchymal Stromal Cells Seeded in a Collagen Scaffold : A Thermodynamic Near-Equilibrium Linear System Modified by the Tripeptide Arg-Gly-Asp (RGD)” ». Journal of Stem Cells Research, Development & ; Therapy 7, n^o 3 (10 septembre 2021) : 1–4. http://dx.doi.org/10.24966/srdt-2060/100075.

Texte intégral

Résumé :

Mesenchymal Stem Cells (MSCs) are multipotent stromal cells found in bone marrow and have the capacity to differentiate into myofibroblast. In contractile myofibroblasts, the molecular motor is the non-muscle myosin (NMIIA) which differs from the muscle myosin by its ultra-slow kinetics. The differentiation of MSCs into myofibroblasts is promoted by the “Transforming Growth Factor” (TGF-b) which represents a potentially target against tissue fibrosis and cancer.

Styles APA, Harvard, Vancouver, ISO, etc.

Seow, Chun Y. « Hill’s equation of muscle performance and its hidden insight on molecular mechanisms ». Journal of General Physiology 142, n^o 6 (25 novembre 2013) : 561–73. http://dx.doi.org/10.1085/jgp.201311107.

Texte intégral

Résumé :

Muscles shorten faster against light loads than they do against heavy loads. The hyperbolic equation first used by A.V. Hill over seven decades ago to illustrate the relationship between shortening velocity and load is still the predominant method used to characterize muscle performance, even though it has been regarded as purely empirical and lacking precision in predicting velocities at high and low loads. Popularity of the Hill equation has been sustained perhaps because of historical reasons, but its simplicity is certainly attractive. The descriptive nature of the equation does not diminish its role as a useful tool in our quest to understand animal locomotion and optimal design of muscle-powered devices like bicycles. In this Review, an analysis is presented to illustrate the connection between the historic Hill equation and the kinetics of myosin cross-bridge cycle based on the latest findings on myosin motor interaction with actin filaments within the structural confines of a sarcomere. In light of the new data and perspective, some previous studies of force–velocity relations of muscle are revisited to further our understanding of muscle mechanics and the underlying biochemical events, specifically how extracellular and intracellular environment, protein isoform expression, and posttranslational modification of contractile and regulatory proteins change the interaction between myosin and actin that in turn alter muscle force, shortening velocity, and the relationship between them.

Styles APA, Harvard, Vancouver, ISO, etc.

Lecarpentier, Yves, Vincent Kindler, Xénophon Krokidis, Marie-Luce Bochaton-Piallat, Victor Claes, Jean-Louis Hébert, Alexandre Vallée et Olivier Schussler. « Statistical Mechanics of Non-Muscle Myosin IIA in Human Bone Marrow-Derived Mesenchymal Stromal Cells Seeded in a Collagen Scaffold : A Thermodynamic Near-Equilibrium Linear System Modified by the Tripeptide Arg-Gly-Asp (RGD) ». Cells 9, n^o 6 (21 juin 2020) : 1510. http://dx.doi.org/10.3390/cells9061510.

Texte intégral

Résumé :

Mesenchymal stromal cells (MSCs) were obtained from human bone marrow and amplified in cultures supplemented with human platelet lysate. Once semi-confluent, cells were seeded in solid collagen scaffolds that were rapidly colonized by the cells generating a 3D cell scaffold. Here, they acquired a myofibroblast phenotype and when exposed to appropriate chemical stimulus, developed tension and cell shortening, similar to those of striated and smooth muscle cells. Myofibroblasts contained a molecular motor—the non-muscle myosin type IIA (NMMIIA) whose crossbridge (CB) kinetics are dramatically slow compared with striated and smooth muscle myosins. Huxley’s equations were used to determine the molecular mechanical properties of NMMIIA. Thank to the great number of NMMIIA molecules, we determined the statistical mechanics (SM) of MSCs, using the grand canonical ensemble which made it possible to calculate various thermodynamic entities such as the chemical affinity, statistical entropy, internal energy, thermodynamic flow, thermodynamic force, and entropy production rate. The linear relationship observed between the thermodynamic force and the thermodynamic flow allowed to establish that MSC-laden in collagen scaffolds were in a near-equilibrium stationary state (affinity ≪ RT), MSCs were also seeded in solid collagen scaffolds functionalized with the tripeptide Arg-Gly-Asp (RGD). This induced major changes in NMMIIA SM particularly by increasing the rate of entropy production. In conclusion, collagen scaffolds laden with MSCs can be viewed as a non-muscle contractile bioengineered tissue operating in a near-equilibrium linear regime, whose SM could be substantially modified by the RGD peptide.

Styles APA, Harvard, Vancouver, ISO, etc.

Holmes, K. C., D. R. Trentham, R. Simmons, H. Lee Sweeney et Anne Houdusse. « The motor mechanism of myosin V : insights for muscle contraction ». Philosophical Transactions of the Royal Society of London. Series B : Biological Sciences 359, n^o 1452 (29 décembre 2004) : 1829–42. http://dx.doi.org/10.1098/rstb.2004.1576.

Texte intégral

Résumé :

It is 50 years since the sliding of actin and myosin filaments was proposed as the basis of force generation and shortening in striated muscle. Although this is now generally accepted, the detailed molecular mechanism of how myosin uses adenosine triphosphate to generate force during its cyclic interaction with actin is only now being unravelled. New insights have come from the unconventional myosins, especially myosin V. Myosin V is kinetically tuned to allow movement on actin filaments as a single molecule, which has led to new kinetic, mechanical and structural data that have filled in missing pieces of the actomyosin–chemo–mechanical transduction puzzle.

Styles APA, Harvard, Vancouver, ISO, etc.

Plus de sources

Thèses sur le sujet "Mechanics and kinetics of myosin motors"

Ökten, Zeynep. « Single molecule mechanics and the myosin family of molecular motors ». [S.l.] : [s.n.], 2006. http://www.diss.fu-berlin.de/2006/6/index.html.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Iliffe, Cathryn Ann. « The kinetics and mechanics of myosin and subfragment-1 from insect flight muscle ». Thesis, University of York, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.251800.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

MELLI, LUCA. « Kinetics and mechanics of myosin motors from frog skeletal muscle ». Doctoral thesis, 2013. http://hdl.handle.net/2158/798458.

Texte intégral

Résumé :

In questa tesi sono stati sviluppati i protocolli per la produzione e la caratterizzazione dei motori miosinici dal muscolo scheletrico della rana nella prospettiva di un loro utilizzo per la realizzazione di motori ibridi costituiti da schiere di motori molecolari la cui geometria è controllata da superfici nanostrutturate. The work reported in this thesis describes the protocols developed for the production and characterization of myosin motors from frog skeletal muscle with the perspective to using them for the realization of synthetic motors composed by linear arrays of myosin motors the geometry of which is controlled by nanostructured surfaces.

Styles APA, Harvard, Vancouver, ISO, etc.

Ökten, Zeynep [Verfasser]. « Single molecule mechanics and the myosin family of molecular motors / vorgelegt von Zeynep Ökten ». 2006. http://d-nb.info/978571118/34.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Kreuzer, Steven Michael. « On the mechanical response of helical domains of biomolecular machines : computational exploration of the kinetics and pathways of cracking ». Thesis, 2013. http://hdl.handle.net/2152/25156.

Texte intégral

Résumé :

Protein mechanical responses play a critical role in a wide variety of biological phenomena, impacting events as diverse as muscle contraction and stem cell differentiation. Recent advances in both experimental and computational techniques have provided the opportunity to explore protein constitutive properties at the molecular level. However, despite these advances many questions remain about how proteins respond to applied mechanical forces, particularly as a function of load magnitude. In order to address these questions, relatively simple helical structures were computationally tested to determine the mechanisms and kinetics of unfolding at a range of physiologically relevant load magnitudes. Atomically detailed constant force molecular dynamics simulations combined with the Milestoning kinetic analysis framework revealed that the mean first passage time (MFPT) of the initiation of unfolding of long (~16nm) isolated helical domains was a non-monotonic function of the magnitude of applied tensile load. The unfolding kinetics followed a profile ranging from 2.5ns (0pN) to a peak of 3.75ns (20pN) with a decreasing MFPT beyond 40pN reflected by an MFPT of 1ns for 100pN. The application of the Milestoning framework with a coarse-grained network analysis approach revealed that intermediate loads (15pN-25pN) retarded unfolding by opening additional, slower unfolding pathways through non-native [pi]-helical conformations. Analysis of coiled-coil helical pairs revealed that the presence of the second neighboring helix delayed unfolding initiation by a factor of 20, with calculated MFPTs ranging from 55ns (0pN) to 85ns (25pN per helix) to 20ns (100pN per helix). The stability of the coiled-coil domains relative to the isolated helix was shown to reflect a decreased propensity to break flexibility restraining intra-helix hydrogen bonds, thereby delaying [psi] backbone dihedral angle rotation and unfolding. These results show for the first time a statistically determined profile of unfolding kinetics for an atomically detailed protein that is non-monotonic with respect to load caused by a change in the unfolding mechanism with load. Together, the methods introduced for analyzing the mechanical response of proteins as well as the timescales determined for the initiation of unfolding provide a framework for the determination of the constitutive properties of proteins and non-biological polymers with more complicated geometries.
text

Styles APA, Harvard, Vancouver, ISO, etc.

Chapitres de livres sur le sujet "Mechanics and kinetics of myosin motors"

Garcia, Kristen, Marcus Hock, Vikrant Jaltare, Can Uysalel, Kimberly J. McCabe, Abigail Teitgen et Daniela Valdez-Jasso. « Investigating the Multiscale Impact of Deoxyadenosine Triphosphate (dATP) on Pulmonary Arterial Hypertension (PAH) Induced Heart Failure ». Dans Computational Physiology, 77–90. Cham : Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-05164-7_7.

Texte intégral

Résumé :

Abstract2-deoxy-ATP (dATP) is a myosin activator known to improve cardiac contractile force [1]. In vitro studies have shown that dATP alters the calcium transient profile in addition to the kinetics of the cross-bridge cycle [2]. Furthermore, in vivo studies of transgenic mice with increased production of dATP show elevated left ventricular systolic function [3]. Pulmonary arterial hypertension (PAH) is a rare disease of the pulmonary vasculature in which pressure overload in the right ventricle results in reduced contractile function and right heart failure [4]. We hypothesize that dATP may have a therapeutic effect on PAH-induced heart failure, by improving contractile function and restoring cardiac output and ejection fraction. However, because the effects of dATP cannot easily be assessed experimentally, we propose using a computational multiscale modeling approach to predict cardiac function. By altering parameters in an existing multiscale biventricular cardiac model [5], we were able to reproduce end-systolic and end-diastolic pressures and volumes that reflect the PAH condition, as well as healthy hearts. dATP was simulated by adjusting parameters in the model at the molecular and cellular levels based on experimental data [1], allowing us to predict the effects of dATP on PAH at the organ level. Our results show that the molecular effects of dATP can increase cardiac output and restore ejection fraction in PAH conditions, though at the cost of elevated mean arterial pressure, and may provide a new approach to treating this disease. Our multiscale modeling approach paves the way for further studies mapping out cardiovascular mechanics. As novel therapeutics continue to be discovered, their application and mechanism can be further explored through these computational models.

Styles APA, Harvard, Vancouver, ISO, etc.

Goldman, Y. E., et E. M. Ostap. « 4.9 Myosin Motors : Kinetics of Myosin ». Dans Comprehensive Biophysics, 151–69. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-374920-8.00411-2.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Actes de conférences sur le sujet "Mechanics and kinetics of myosin motors"

Bidone, Tamara Carla, Haosu Tang et Dimitrios Vavylonis. « Insights Into the Mechanics of Cytokinetic Ring Assembly Using 3D Modeling ». Dans ASME 2014 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2014. http://dx.doi.org/10.1115/imece2014-39006.

Texte intégral

Résumé :

During fission yeast cytokinesis, actin filaments nucleated by cortical formin Cdc12 are captured by myosin motors bound to a band of cortical nodes. The myosin motors exert forces that pull nodes together into a contractile ring. Cross-linking interactions help align actin filaments and nodes into a single bundle. Mutations in the myosin motor domain and changes in the concentration of cross-linkers alpha-actinin and fimbrin alter the morphology of the condensing network, leading to clumps, rings or extended meshworks. How the contractile tension developing during ring formation depends on the interplay between network morphology, myosin motor activity, cross-linking and actin filament turnover remains to be elucidated. We addressed this question using a 3D computational model in which semiflexible actin filaments (represented as beads connected by springs) grow from formins, can be captured by myosin in neighboring nodes, and get cross-linked with one another through an attractive interaction. We identify regimes of tension generation between connected nodes under a wide set of conditions regarding myosin dynamics and strength of cross-linking between actin filaments. We find conditions that maximize circumferential tension, correlate them with network morphology and propose experiments to test these predictions. This work addresses “Morphogenesis of soft and living matter” using computational modeling to simulate cytokinetic ring assembly from the key molecular mechanisms of viscoelastic cross-linked actin networks that include active molecular motors.

Styles APA, Harvard, Vancouver, ISO, etc.

Egan, Paul F., Philip R. LeDuc, Jonathan Cagan et Christian Schunn. « A Design Exploration of Genetically Engineered Myosin Motors ». Dans ASME 2011 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/detc2011-48568.

Texte intégral

Résumé :

As technology advances, there is an increasing need to reliably output mechanical work at smaller scales. At the nanoscale, one of the most promising routes is utilizing biomolecular motors such as myosin proteins commonly found in cells. Myosins convert chemical energy into mechanical energy and are strong candidates for use as components of artificial nanodevices and multi-scale systems. Isoforms of the myosin superfamily of proteins are fine-tuned for specific cellular tasks such as intracellular transport, cell division, and muscle contraction. The modular structure that all myosins share makes it possible to genetically engineer them for fine-tuned performance in specific applications. In this study, a parametric analysis is conducted in order to explore the design space of Myosin II isoforms. The crossbridge model for myosin mechanics is used as a basis for a parametric study. The study sweeps commonly manipulated myosin performance variables and explores novel ways of tuning their performance. The analysis demonstrates the extent that myosin designs are alterable. Additionally, the study informs the biological community of gaps in experimentally tabulated myosin design parameters. The study lays the foundation for further progressing the design and optimization of individual myosins, a pivotal step in the eventual utilization of custom-built biomotors for a broad range of innovative nanotechnological devices.

Styles APA, Harvard, Vancouver, ISO, etc.

Nous offrons des réductions sur tous les plans premium pour les auteurs dont les œuvres sont incluses dans des sélections littéraires thématiques. Contactez-nous pour obtenir un code promo unique!