Functional Mechanisms of ABC Transporters as Revealed by Molecular Simulations

2018 ◽  
pp. 179-201 ◽  
Author(s):  
Tadaomi Furuta ◽  
Minoru Sakurai
Keyword(s):  
Abc Transporters ◽  
Molecular Simulations ◽  
Functional Mechanisms

Computer simulations of ABC transporter componentsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.

2006 ◽  
Vol 84 (6) ◽  
pp. 900-911 ◽  
Author(s):  
Eliud O. Oloo ◽  
Christian Kandt ◽  
Megan L. O’Mara ◽  
D. Peter Tieleman
Keyword(s):  
Abc Transporters ◽  
Simulation Techniques ◽  
Multiple Components ◽  
Functional Dynamics ◽  
Future Challenges ◽  
Health And Disease ◽  
Dynamics Simulations ◽  
Functional Mechanisms ◽  
Computer Simulation Techniques ◽  
Selection Of

Current computer simulation techniques provide robust tools for studying the detailed structure and functional dynamics of proteins, as well as their interaction with each other and with other biomolecules. In this minireview, we provide an illustration of recent progress and future challenges in computer modeling by discussing computational studies of ATP-binding cassette (ABC) transporters. ABC transporters have multiple components that work in a well coordinated fashion to enable active transport across membranes. The mechanism by which members of this superfamily execute transport remains largely unknown. Molecular dynamics simulations initiated from high-resolution crystal structures of several ABC transporters have proven to be useful in the investigation of the nature of conformational coupling events that may drive transport. In addition, fruitful efforts have been made to predict unknown structures of medically relevant ABC transporters, such as P-glycoprotein, using homology-based computational methods. The various techniques described here are also applicable to gaining an atomically detailed understanding of the functional mechanisms of proteins in general.

Tubulin structure at intermediate resolution

1995 ◽  
Vol 53 ◽  
pp. 852-853
Author(s):  
K. H. Downing ◽  
S. G. Wolf ◽  
E. Nogales
Keyword(s):  
High Resolution ◽  
Structural Data ◽  
Therapeutic Drug ◽  
Zinc Ions ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray ◽  
Negative Stain ◽  
Functional Mechanisms ◽  
Tubulin Structure

Microtubules are involved in a host of critical cell activities, many of which involve transport of organelles through the cell. Different sets of microtubules appear to form during the cell cycle for different functions. Knowledge of the structure of tubulin will be necessary in order to understand the various functional mechanisms of microtubule assemble, disassembly, and interaction with other molecules, but tubulin has so far resisted crystallization for x-ray diffraction studies. Fortuitously, in the presence of zinc ions, tubulin also forms two-dimensional, crystalline sheets that are ideally suited for study by electron microscopy. We have refined procedures for forming the sheets and preparing them for EM, and have been able to obtain high-resolution structural data that sheds light on the formation and stabilization of microtubules, and even the interaction with a therapeutic drug.Tubulin sheets had been extensively studied in negative stain, demonstrating that the same protofilament structure was formed in the sheets and microtubules. For high resolution studies, we have found that the sheets embedded in either glucose or tannin diffract to around 3 Å.

An empirical test of situational strength's functional mechanisms

2010 ◽  
Author(s):  
Irwin J. Jose ◽  
Rustin D. Meyer ◽  
Richard Hermida ◽  
Vivek Khare ◽  
Reeshad S. Dalal
Keyword(s):  
Empirical Test ◽  
Functional Mechanisms

Developments in 3D Echocardiography

2009 ◽  
Vol 5 (2) ◽  
pp. 10 ◽  
Author(s):  
Jose Luis Zamorano ◽  
Keyword(s):  
3D Echocardiography ◽  
Resonance Imaging ◽  
Clinical Tool ◽  
3D Images ◽  
Processing Power ◽  
2D Echocardiography ◽  
Automated Quantification ◽  
Heart Cycle ◽  
Functional Mechanisms ◽  
Full Volume

3D echocardiography (3DE) will gain increasing acceptance as a routine clinical tool as the technology evolves due to advances in technology and computer processing power. Images obtained from 3DE provide more accurate assessment of complex cardiac anatomy and sophisticated functional mechanisms compared with conventional 2D echocardiography (2DE), and are comparable to those achieved with magnetic resonance imaging. Many of the limitations associated with the early iterations of 3DE prevented their widespread clinical application. However, recent significant improvements in transducer and post-processing software technologies have addressed many of these issues. Furthermore, the most recent advances in the ability to image the entire heart in realtime and fully automated quantification have poised 3DE to become more ubiquitous in clinical routine. Realtime 3DE (RT3DE) systems offer further improvements in the diagnostic and treatment planning capabilities of cardiac ultrasound. Innovations such as the ability to acquire non-stitched, realtime, full-volume 3D images of the heart in a single heart cycle promise to overcome some of the current limitations of current RT3DE systems, which acquire images over four to seven cardiac cycles, with the need for gating and the potential for stitch artefacts.

Split the Charge Difference in Two! a Rule of Thumb for Adding Proper Amounts of Ions in MD Simulations

2020 ◽  
Author(s):  
Matías R. Machado ◽  
Sergio Pantano
Keyword(s):  
Molecular Dynamics ◽  
Ionic Strength ◽  
Molecular Simulations ◽  
Md Simulations ◽  
Good Practices ◽  
Rule Of Thumb ◽  
Ionic Concentrations

<p> Despite the relevance of properly setting ionic concentrations in Molecular Dynamics (MD) simulations, methods or practical rules to set ionic strength are scarce and rarely documented. Based on a recently proposed thermodynamics method we provide an accurate rule of thumb to define the electrolytic content in simulation boxes. Extending the use of good practices in setting up MD systems is promptly needed to ensure reproducibility and consistency in molecular simulations.</p>

On the Use of Quantum Thermal Bath in Unimolecular Fragmentation Simulations

2019 ◽  
Author(s):  
Riccardo Spezia ◽  
Hichem Dammak
Keyword(s):  
Degrees Of Freedom ◽  
Molecular Simulations ◽  
Zero Point ◽  
Thermal Bath ◽  
Unimolecular Dissociation ◽  
Point Energy ◽  
Rotational Degrees Of Freedom ◽  
The Difference ◽  
Nuclear Effects

<div> <div> <div> <p>In the present work we have investigated the possibility of using the Quantum Thermal Bath (QTB) method in molecular simulations of unimolecular dissociation processes. Notably, QTB is aimed in introducing quantum nuclear effects with a com- putational time which is basically the same as in newtonian simulations. At this end we have considered the model fragmentation of CH4 for which an analytical function is present in the literature. Moreover, based on the same model a microcanonical algorithm which monitor zero-point energy of products, and eventually modifies tra- jectories, was recently proposed. We have thus compared classical and quantum rate constant with these different models. QTB seems to correctly reproduce some quantum features, in particular the difference between classical and quantum activation energies, making it a promising method to study unimolecular fragmentation of much complex systems with molecular simulations. The role of QTB thermostat on rotational degrees of freedom is also analyzed and discussed. </p> </div> </div> </div>

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