News and Updates

Highlights and overview of selected recent Consortium-sponsored publications

Biomolecular DNP- supported NMR spectroscopy using site directed spin labeling

Authors: Elwin A.W. van der Cruijsen, Eline J. Koers, Claire Sauvee, Raymond E. Hulse, Markus Weingarth, Olivier Ouari, Eduardo Perozo, Paul Tordo, and Marc Baldus.

In the press, Journal of the American Chemical Society. (Consortium project: Dynamics of Ion Permeation and Conformation Coupling in KcsA)

Molecular probes that combine the benefits of enhanced spectroscopic sensitivity with site-specific localization have significantly expanded our ability to track molecular structure and function in applications ranging from cell biology to material science . In the field of magnetic resonance, dynamic nuclear polarization (DNP) has become a widely usable method to significantly enhance overall spectroscopic sensitivity in NMR and MRI. Here, the authors show that DNP can be established by creating local spin clusters via site-directed spin labeling using mono- or biradicals. Applied to a membrane-embedded potassium channel, we show that this approach can significantly enhance NMR sensitivity while preserving the intrinsic spectroscopic properties of (bi)radicals as paramagnetic relaxation enhancers.

The results suggest that the creation of local spin clusters can generate sizable DNP enhancements while preserving the intrinsic benefits of PRE-based NMR approaches. Our results are consistent with the idea that the magnitude in DNP enhancement are highly dependent on the nearest neighbor electron-electron distances.

13C NMR detects conformational change in the 100-kD membrane transporter Cl-C-ec1

Authors: Sherwin J. Abraham, Ricky C. Cheng, Thomas A. Chew, Chandra M. Khantwal, Corey W. Liu, Shimei Gong, Robert K. Nakamoto, and Merritt Maduke.

J Biomol NMR. 2015 Jan 29. (Consortium project: Conformational Dynamics in the CLC Channel Transporter Family. Consortium core: Membrane Protein Production)

Members of the Cl-C (‘‘Chloride-Channel’’) family play central roles in cardiovascular, neuronal, bone, and epithelial function. Cl-C transporters catalyze the exchange of Cl--for H+ across cellular membranes. To do so, they must couple Cl-- and H+ binding and unbinding to protein conformational change. However, the sole conformational changes distinguished crystallographically are small movements of a glutamate side chain that locally gates the ion transport pathways. Therefore, our understanding of whether and how global protein dynamics contribute to the exchange mechanism has been severely limited. To overcome the limitations of crystallography, the authors used solution-state 13Cmethyl NMR with labels on methionine, lysine, and engineered cysteine residues to investigate substrate (H+) dependent conformational change outside the restraints of crystallization. They show that methyl labels in several regions report H+-dependent spectral changes. They  identify one of these regions as Helix R, a helix that extends from the center of the protein, where it forms the part of the inner gate to the Cl-–permeation pathway, to the extracellular solution. The H+-dependent spectral change does not occur when a label is positioned just beyond Helix R, on the unstructured C-terminus of the protein.

Together, the results suggest that H+ binding is mechanistically coupled to Cl-osing of the intracellular access-pathway for Cl--. These studies set the stage for investigating the structural details and dynamics of this change.

Room-Temperature Distance Measurements of Immobilized Spin-Labeled Protein by DEER/PELDOR

Authors: Virginia Meyer, Michael A. Swanson, Laura J. Clouston, Przemyslaw J. Boratynski, Richard A. Stein, Hassane S. Mchaourab, Andrzej Rajca, Sandra S. Eaton, and Gareth R. Eaton.

Biophys J. 2015 Mar 10;108(5):1213-9. (Consortium Core: Membrane Protein Production)

Nitroxide spin labels are used for double electron-electron resonance (DEER) measurements of distances between sites in biomolecules. Rotation of gem-dimethyls in commonly used nitroxides causes spin echo dephasing times (Tm) to be too short to perform DEER measurements at temperatures between ~80 and 295 K, even in immobilized samples. A spirocyclohexyl spin label has been prepared that has longer Tm between 80 and 295 K in immobilized samples than conventional labels. Two of the spirocyclohexyl labels were attached to sites on T4 lysozyme introduced by site-directed spin labeling. Interspin distances up to ~4 nm were measured by DEER at temperatures up to 160 K in water/glycerol glasses. In a glassy trehalose matrix the Tm for the doubly labeled T4 lysozyme was long enough to measure an interspin distance of 3.2 nm at 295 K, which could not be measured for the same protein labeled with the conventional 1-oxyl-2,2,5,5-tetramethyl-3-pyrroline-3-(methyl) methanethio-sulfonate label.

The leap from 80 K DEER measurements to room temperature is an important step toward DEER measurement in physiological environments. The current fundamental requirement for DEER of protein immobilization provides additional avenues toward improvement of the technique.

Architecture of the nuclear pore complex coat

Authors: Tobias Stuwe, Ana R. Correia, Daniel H. Lin, Marcin Paduch, Vincent T. Lu, Anthony A. Kossiakoff, and André Hoelz.

Science. 2015 Mar 6;347(6226):1148-52. (Consortium core: Synthetic Antigen Binder (SAB) Generation and Crystallography)

The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. Despite half a century of structural characterization, the architecture of the NPC remains unknown. In this research report, the authors present the crystal structure of a reconstituted ~400-kilodalton coat nucleoporin complex (CNC) from Saccharomyces cerevisiae at a 7.4 angstrom resolution. The crystal structure revealed a curved Y-shaped architecture and the molecular details of the coat nucleoporin interactions forming the central “triskelion” of the Y. A structural comparison of the yeast CNC with an electron microscopy reconstruction of its human counterpart suggested the evolutionary conservation of the elucidated architecture. Moreover, 32 copies of the CNC crystal structure docked readily into a cryoelectron tomographic reconstruction of the fully assembled human NPC, thereby accounting for ~16 megadalton of its mass.

Multilevel Summation Method for Electrostatic Force Evaluation

Authors: David J. Hardy, Zhe Wu, James C. Phillips, John E. Stone, Robert D. Skeel, and Klaus Schulten.

J Chem Theory Comput. 2015 Feb 10;11(2):766-779. PMCID: PMC4325600. (Consortium core: Computational Modeling Core)

Significant long-range electrostatic interactions arise in many biomolecular systems, such as negatively charged DNA and RNA, polar or charged membranes, ion channels, and electrostatic steering of protein−protein and enzyme−substrate association. Accordingly, electrostatic interactions need to be accurately represented in molecular modeling calculations. The computational cost increases in principle as N2, where N is the number of charged partiCl-es in the system.

The multilevel summation method (MSM) offers an efficient algorithm utilizing convolution for evaluating long-range forces arising in molecular dynamics simulations. Shifting the balance of computation and communication, MSM provides key advantages over the ubiquitous partiCl-e−mesh Ewald (PME) method, offering better scaling on parallel computers and permitting more modeling flexibility, with support for periodic systems as does PME but also for semiperiodic and nonperiodic systems. The version of MSM available in the simulation program NAMD is described, and its performance and accuracy are compared with the PME method. The accuracy feasible for MSM in practical applications reproduces PME results for water property calculations of density, diffusion constant, dielectric constant, surface tension, radial distribution function, and distance dependent Kirkwood factor, even though the numerical accuracy of PME is higher than that of MSM. Excellent agreement between MSM and PME is found also for interface potentials of air−water and membrane−water interfaces, where long-range Coulombic interactions are crucial. Applications demonstrate also the suitability of MSM for systems with semiperiodic and nonperiodic boundaries. For this purpose, simulations have been performed with periodic boundaries along directions parallel to a membrane surface but not along the surface normal, yielding membrane pore formation induced by an imbalance of charge across the membrane. Using a similar semiperiodic boundary condition, ion conduction through a graphene nanopore driven by an ion gradient has been simulated. Furthermore, proteins have been simulated inside a single spherical water droplet. Finally, parallel scalability results show the ability of MSM to outperform PME when scaling a system of modest size (less than 100 K atoms) to over a thousand processors, demonstrating the suitability of MSM for large-scale parallel simulation.

Ongoing is the development of improved interpolation for MSM to provide higher accuracy for a given polynomial degree p without increasing the computational cost. Future work inCl-udes also the calculation of dispersion forces without truncation with MSM-based NAMD; these forces, in particular, their long-range contribution, are considered to be important for membrane properties. With support in NAMD also for long-range dispersion forces, the present CHARMM-prescribed 12 Å cutoff/splitting distance can be used as a true control for MSM accuracy. High performance simulations will then be able to achieve practical accuracy with a reduced splitting distance, where a splitting distance of between 8 and 9 Å is expected to double the overall simulation performance.

Potential Application of Alchemical Free Energy Simulations to Discriminate GPCR Ligand Efficacy

Authors: Hui Sun Lee, Chaok Seok, and Wonpil Im.

J. Chem. Theory Comput. 2015 Feb 10;11:1255-1266. (Consortium core: Computational Modeling Core)

G protein-coupled receptors (GPCRs) constitute the largest protein superfamily in the human genome with almost 1,000  members. They play key functional roles as major contributors of information flow from the outside to the inside of the cell, making them one of the most important protein families. As a result of their broad influence on human physiology and behavior, GPCRs are arguably the most promising targets for development of new and more effective therapeutic agents.

Based on the fact that GPCR-mediated signaling is modulated in a ligand-specific manner such as agonist, inverse agonist, and neutral antagonist (termed ligand efficacy), quantitative characterization of the ligand efficacy is essential for rational design of selective modulators for GPCR targets. As experimental approaches for this purpose are time-, cost-, and labor-intensive, computational tools that can systematically predict GPCR ligand efficacy can have a big impact on GPCR drug design. Here, the authors have performed free energy perturbation molecular dynamics simulations to calculate absolute binding free energy of an inverse agonist, a neutral antagonist, and an agonist to β2-adrenergic receptor (β2-AR) active and inactive states, respectively, in explicit lipid bilayers. Relatively short alchemical free energy calculations reveal that both the time series of the total binding free energy and decomposed energy contributions can be used as relevant physical properties to discriminate β2-AR ligand efficacy. This study illustrates a merit of the current approach over simple, fast docking calculations or highly expensive millisecond-time scale simulations.

It is the authors’ hope that their computational approach improves research and development efficiency in designing novel lead compounds targeting various GPCRs for the treatment of various human diseases.

Publication by S.M. Islam and B. Roux about spin-labels selected for J. Phys. Chem. B cover illustration

A publication by Computational Modeling Core participant Benoît Roux and postdoc Shahidul Islam titled “Simulating the Distance Distribution between Spin-Labels Attached to Proteins,” published in Journal of Physical Chemistry B 119(10) on February 2nd, was selected as the cover illustration for that issue.

Cover Art: Simplified representation of spin-labels inserted in protein were used in molecular dynamics (MD) simulation to obtain spin-pair distance distributions that could be directly compared to those obtained from EPR/DEER for the validation of the structural models of proteins and the simplified spin-labels could also be used in restrained-ensemble MD simulation for the structural refinement of proteins by using the EPR/DEER distance distribution data.

Room reservations now available at the DoubleTree Hotel

DoubleTree by Hilton Chicago – Magnificent Mile
300 East Ohio Street, Chicago, IL 60611 (Map and Directions)
Website: http://DoubleTreeMagMile.com
Phone: (312) 787-6100

Hotel fact sheet: http://www.doubletreemagmile.com/files/940/DoubleTree_Chicago_Mag_Mile_Fact_Sheet.pdf

The Consortium will cover all related costs for the Consortium PI and one postdoc/student. Any additional attendees will be responsible for covering all costs related to the meeting.

A block of rooms has been reserved under the name of MPSDC 2015 Annual Meeting for additional attendees from April 28 to May 1st. Please visit this page to access reservations under this block (group code: UCG)

If you have any questions about booking, please contact Lisa Anderson at landerso@bsd.uchicago.edu.

MPSDC 2015 Annual Meeting program now available

The program for the MPSDC 2015 Annual Meeting has been posted to the website. Please visit the program page to see the schedule for each day.

MPSDC 2015 Annual Meeting announced

MPSDC 2013 Annual Meeting attendees at the Gleacher Center

The Membrane Protein Structural Dynamics (MPSDC) 2015 Annual Meeting website has been launched, and we are ready to receive registrations! Please note that unlike last year’s Frontiers in Membrane Protein Dynamics conference, this annual meeting is open to Consortium participants and invited guests only.

Program at a glance

The Gleacher Center, Chicago IL

DAY 1: Wednesday, April 29th
1:00pm-5:00pm | Workshop: Exploring the Interface Between Computation and Experiment

DAY 2: Thursday, April 30th
8:30am-5:00pm | Scientific Sessions

DAY 3: Friday, May 1st
8:00am-12:30pm | Featured Talks

View Full Program »

Register »

Consortium members to participate in Biophysical Society 59th Annual Meeting symposia, workshops, and national lecture


MPSDC Awards: Francisco Bezanilla, Past President presenting an award to Robert Nakamoto.
(Click to enlarge)

The Membrane Protein Structural Dynamics Consortium is always very well represented at the annual Biophysical Society meeting, with Consortium members actively involved at the leadership level, including Francisco Bezanilla‘s tenure as president from 2012 to 2014, as well as at the level of participants in a remarkably large number of workshops, symposia, and presentations.

At next year’s meeting in Baltimore, MPSDC members will participate in a number of specialty symposia and workshops organized by the Biophysical society (more information on the nature of these symposia and workshops can be found on the Biophysical Society meeting website here). We would like to highlight the following in particular (though there are and will certainly be more ways in which Consortium members are involved with the meeting):

  • Emad Tajkhorshid (UIUC) will be chairing the Permeation & Transport Subgroup 2015 Symposium. He is also chairing a workshop on Advances in Computing Large Systems.
  • Olga Boudker (Weill Cornell Medical College) is chairing a symposium on Neurotransmitter Transporters.
  • Christopher Ahern (University of Iowa) is participating in a symposium on Probing Ion Channel Structure/Function Using Novel Tools.
  • Jamies Bowie (UCLA) is participating in a workshop on Stabilizing Membrane Proteins.
  • Ivet Bahar (UPittsburgh) is giving a lecture titled “Neurotransmitter Translocation: Insights from Network Models and Multiscale Simulations” at the Biopolymers in Vivo Subgroup 2015 Symposium.
  • José Faraldo Gómez (NIH and MPSDC Associate Member) is giving a lecture titled “Novel Insights into the Structure and Mechanism of Proton and Sodium/Calcium Exchangers” at the Membrane Biophysics Subgroup 2015 Symposium.

Last but not least, MPSDC member and one of our keynote speakers at Frontiers in Membrane Protein Structural Dynamics 2014 Klaus Schulten (UIUC) will give the prestigious National Lecture. The National Lecturer is the highest award given each year by the Biophysical Society. The recipient presents the National Lecture on Monday evening of the Annual Meeting. We would like to congratulate Dr. Schulten on achieving this great honor.

See also: interviews from last year’s Biophysical Society with Francisco Bezanilla, Past President and Robert Nakamoto, Chair of the 2014 BPS Program Committee.

CHARMM-GUI Membrane Builder publication by Im et al. featured as cover image for Journal of Computational Chemistry


Dr. Wonpil Im, University of Kansas

One of the ongoing projects in the laboratory of Wonpil Im (University of Kansas and MPSDC team member) has been to contribute to the development of CHARMM-GUI and CHARMM-GUI modules, such as the Ligand Binder and the Membrane Builder. These tools help users generate a series of CHARMM inputs towards a specific purpose, like calculating a protein/ligand binding free energy or building a protein/membrane complex for molecular dynamics simulations. The Consortium’s Computational Modeling Core has provided partial support for the completion of such modules.

Im and his team recently published a paper about the Membrane Builder module in Journal of Computational Chemistry, titled “CHARMM-GUI Membrane Builder toward realistic biological membrane simulations” (reference below). This publication was featured as the cover image for the issue, which can be viewed below. J Comput Chem attached the following note about the article’s relevance:

On page 1997 (DOI: 10.1002/jcc.23712), Emilia L. Wu, Xi Cheng, Sunhwan Jo, Huan Rui, Kevin C. Song, Eder M. Dávila‐Contreras, Yifei Qi, Jumin Lee, Viviana Monje‐Galvan, Richard M. Venable, Jeffery B. Klauda, and Wonpil Im report on the CHARMM‐GUI Membrane Builder, a web‐based user interface designed to interactively build all‐atom protein/membrane or membrane‐only systems for molecular dynamics simulation through an automated optimized process. The cover image illustrates the building process of a protein/membrane system by reading the protein structure, generating pore water/bilayer/bulk water/ions, and combining all the components.


(Click to enlarge)

Reference:

Wu EL, Cheng X, Jo S, Rui H, Song KC, Dávila-Contreras EM, Qi Y, Lee J, Monje-Galvan V, Venable RM, Klauda JB, Im W. CHARMM-GUI Membrane Builder toward realistic biological membrane simulations. J Comput Chem. 2014 Oct 15;35(27):1997-2004. PMID: 25130509. PMCID: PMC4165794 [Available on 2015/10/15].

MPSDC Summer 2014 e-newsletter released


Fresh off the press: we just sent out our second MPSDC e-newsletter, covering the successful Frontiers in Membrane Protein Structural Dynamics 2014 held in Chicago last month, new resources provided by the Computational Modeling Core, and several of the latest research advances sponsored by the Consortium.

We invite you to sign up for our mailing list, in order to stay up to date with the latest information pertaining to the Membrane Protein Structural Dynamics Consortium (MPSDC). Through our mailing list, we will provide updates about our conferences, meetings and workshops, and send out a semi-annual newsletter aggregating all of the latest content on the website.

Sign up here »

To view archived e-newsletters, please visit the previous link.

Thank you for attending Frontiers in Membrane Protein Structural Dynamics 2014

On May 7th, 8th, and 9th, the Membrane Protein Structural Dynamics Consortium (MPSDC) held its second Frontiers in Membrane Protein Structural Dynamics meeting at the Chicago Hilton Hotel. The meeting featured both Consortium members and external invitees, and consisted of eight scientific sessions, poster presentations (and mandatory one-minute Flash! Poster talks), as well as two keynote lectures by Robert Stroud (UCSF) and Klaus Schulten (UIUC). Prior to the conference, the MPSDC hosted several satellite events including a computational modeling workshop, a mini-symposium meeting concerning the latest advances in computational approaches, and a workshop on spectroscopy methodologies.

Satellite events (May 6th and 7th)



Eric Lindhal, Stockholm University and KTH Royal Institute of Technology

As in previous years, the MPSDC’s Computational Modeling Core hosted a membrane protein modeling workshop, and a computational mini-symposium concerning the latest advances in computational approaches to the study of membrane proteins. The computational modeling workshop was co-chaired by Emad Tajkhorshid (UIUC) and Wonpil Im (University of Kansas) and provided attendants with an overview of the use of the modeling dynamics and visualization software NAMD and VMD, as wel as the CHARMM-GUI Membrane Builter and force field parameterization tools. Jeff Klauda (University of Maryland) was also invited to speak about lipid bilayer simulations. This year’s mini-symposium was chaired by Benoît Roux (University of Chicago) and covered a number of topics including methodologies and their applications, voltage gating, and pumps and transporters.

This year, the Consortium also organized a spectroscopy workshop, co-chaired by Marc Baldus (Utrecht University) and Yeon-Kyun Shin (Iowa State University). This workshop featured both Consortium collaborators and invited speakers, including Ana Correa (University of Chicago), Tae-Young Yoon (Korean Advanced Institute of Science and Technology), Martin Zanni (University of Wisconsin), Gary Lorigan (Miami University), and Daniella Goldfarb (Weizmann Institute). Topics discussed at this workshop focused on addressing techiques in solid-state and solution NMR, EPR including DEER approaches, infrared, fluorescence and single molecule techniques including magnetic tweezers. Both workshops and minisymposium were well attended and productive, and we will continue to host such satellite events in the future.

Keynote Lectures

For the first time, we invited two premier scientists in the field of membrane protein biophysics to give a keynote lecture at the meeting.

Our first keynote speaker was Robert Stroud, Professor of Biochemistry & Biophysics and Pharmaceutical Chemistry at the University of California at San Francisco. At the Stroud lab, scientists seek to understand molecular mechanisms of certain key biological processes, as well as signal transduction between processes at the level of protein structure, dynamics, and mechanism. In addition to his posting at UCSF, Dr. Stroud is also the director of the Membrane Protein Expression Center, one of the centers funded by the NIH Common Fund Structural Biology Program. The MPEH develops and applies the latest innovative methods yielding structurally and functionally intact eukaryotic membrane proteins for drug development, and structural and functional characterization.

Stroud’s lecture was titled Wiggle wiggle – not a trickle: How do Membrane transporters work (to concentrate ions 1000 fold)? In his lecture, Stroud discussed how secondary transporters can drive and concentrate nutrients or ions ‘uphill’ (energetically) across membranes achieving gradients of >1000:1 driven by ‘downhill’ movement of other coupled ions, protons, metabolites or electrochemical gradients.

Our second keynote speaker was one of our very own Consortium members: Klaus Schulten, Swanlund Professor of Physics at the University of Illinois at Urbana Champaign. Professor Schulten is a full-time faculty member in the Beckman Institute and directs the Theoretical and Computational Biophysics Group. His professional interests are theoretical physics and theoretical biology. His current research focuses on the structure and function of supramolecular systems in the living cell, and on the development of non-equilibrium statistical mechanical descriptions and efficient computing tools for structural biology. Professor Schulten is a leader in the field of computational biophysics, having devoted over 40 years to establishing the physical mechanisms underlying processes and organization in living systems from the atomic to the organism scale. Schulten is a strong proponent of the use of simulations as a “computational microscope”, to augment experimental research, and to lead to discoveries that could not be made through experiments so far. The molecular dynamics and structure analysis programs NAMD and VMD, born and continuously developed in his group, are used today by many thousands of researchers across the world.



Karen Fleming, Johns Hopkins University

Schulten’s lecture was titled The photosynthetic membrane of purple bacteria – An amazing clockwork of proteins and processes. Schulten described a spherical bioenergetic membrane in purple bacteria of 70nm diameter involving 130 protein complexes called the chromatophore. Hundreds of chromatophores provide a bacterium with energy in the form of ATP, the synthesis of ATP being driven by sun light. The overall function in each chromatophore comes about through a clockwork of intertwined physical processes. Schulten presented a computational description of the subprocesses (using the programs NAMD and PHI as well as quantum chemical programs) along with advanced molecular graphics (using the program VMD), in so doing offering an extremely detailed views of the processes mentioned.

Schulten showed a VMD-produced video during his lecture, which can be viewed here along with the audio from his keynote lecture. Additionally, we interviewed Schulten about his keynote and a number of other topics prior to the meeting; this interview can be accessed here.

Poster presentations and Flash! Poster Talks

Post-docs and graduate students attending the meeting were invited to bring posters to the meeting, which were displayed in a dedicated room at the Chicago Hilton Hotel. A total number of fifty-two posters were brought to the meeting, representing twenty different institutions and covering an extensive range of topics relating to cutting edge scientific research on membrane proteins. Each of the 52 presenters were asked to give a one minute Flash! Poster talk based on one powerpoint slide that they were asked to bring. These poster talks took place consecutively on Wednesday night, following Robert Stroud’s keynote lecture.



Harel Weinstein, Weill Cornell Medical College

Many attendees agreed that this was one of the most intellectually engaging parts of the meeting. According to Harel Weinstein (Cornell), “one of the most impressive parts of the meeting were the Flash! presentations of the posters, because it underscored (1) the extraordinary interest of young people, and very talented people in this field, and (2) the enormous breadth of this field, both from the biological point of view, and to a large extent, from a computational point of view.” For Weinstein, the MPSDC’s primary goal was and continues to be to create a bridge between experimental and computational research on membrane proteins, and these poster presentations seemed to directly take on that challenge by featuring an intense, visible cross-pollination between experimentation and computation. The fact that this is “coming together under the umbrella, or at least the sponsorship of the Consortium is a great victory for the Consortium idea,” according to Weinstein. Hassane Mchaourab (Vanderbilt) mentioned being very impressed by the posters both in terms of quantity and quality, and with the Flash! talks “which forced students and post-docs to articulate, in one minute, why their work is important, how does it contribute to the field, and to highlight its significance. And that really advertised the work that was presented in more detail in the posters, so I think that was a really good idea.”

Anatrace graciously sponsored a number of travel awards and poster prizes for students and postdocs attending the meeting. Four travel awards ($500) and two poster prizes were decided by a panel on the basis of merit. Winners of the Anatrace awards were announced at the meeting, and can also be found here.

Scientific Sessions

The bulk of Frontiers in Membrane Protein Structural Dynamics 2014 took place in the form of eight scientific sessions on contemporary issues in membrane protein dynamics. These sessions touched on topics as diverse as protein engineering for conformational dynamics, stability and folding; structural approaches; energy coupling in transporters. computational approaches to membrane protein conformational pathways; structure and dynamics of divalent ion channels and transporters; computational challenges and strategies; voltage sensing; and movement in ligand-gated channels.

As in previous years, we invited both Consortium PI’s and external invitees to foster productive conversations with our colleagues, as well as possible future collaborations. Accordingly, the official meeting program consisted of twenty-five scientists not affiliated with the MPSDC, along with fifteen Consortium team members. To see each of the individual talks, the official program can be viewed here. All panels were well attended and each of the talks were followed by stimulating discussions between speakers and the audience.



Yifan Cheng, University of California, San Francisco

Meeting participants and attendees agreed that this was a productive and valuable meeting. According to Eric Lindhal (Stockholm University), Frontiers in Membrane Protein Structural Dynamics 2014 makes for a “great environment, not just for [research on] simulations or experiments, but really collecting everything that is happening with membrane proteins in the world. I would argue that 75% of the world’s leading groups are in this very room during the meeting.” For Lindhal, the meeting demonstrated that “we’re getting better and better at interfacing simulations very closely with experiment, that experimentalists are getting more involved in running simulations.” Yifan Cheng (UCSF) noted that this was an intense but productive meeting, with many “exciting stories.” Cheng’s group has only recently begun to work on membrane proteins and ion channels, so for him, “this was a great opportunity to be part of the membrane protein structural biology and biophysics community, to get to know people and talk about potential collaborations, and to listen to a lot of wonderful talks from many other labs.”



Hassane Mchaourab, Vanderbilt University.

MPSDC collaborators also spoke highly of the meeting. Hassane Mchaourab described Frontiers in Membrane Protein Structural Dynamics 2014 as an “intense meeting, which brought together some of the major players in the field of membrane protein structure, function and dynamics, and allowed them to discuss the frontier of the field.”

We’d like to thank all who attended and took part in this year’s discussions, and look forward to seeing you at our future meetings!

Below are several photos of the meeting and satellite events. You can either scroll through the photos here or visit the photo set on Flickr. We’ve also made available several brief audio interviews with several conference participants, to be found in the margins of the body of this post. We asked participants about their research, and their views on Frontiers in Membrane Protein Structural Dynamics 2014, what they felt were some of the highlights of the meeting, and if applicable, their recent collaborations with the MPSDC.

Visit the photo set on Flickr »

Anatrace Poster & Travel Award recipients announced

As previously announced, Anatrace has graciously sponsored travel awards and poster prizes for students and postdocs attending the meeting. Four travel awards ($500) and two poster prizes were decided by a panel on the basis of merit. Winners of these awards were announced at the meeting, and can now be released to the public.

The winners of the Anatrace poster & travel awards are:

Poster Awards:

Anne Georges, Washington University of St. Louis
Investigating the inhibitory effects of a novel monobody on EmrE transport activity

Zachary James, University of Minnesota
EPR Detects Changes in the Transmembrane Region of the SERCA-PLB Complex Upon Ser16 Phosphorylation

Travel Awards:

Adam Chamberlin, University of Calgary
The gating pathway in the voltage-gated proton channel

Michael V. LeVine, Weill Cornell Medical College
NbIT – a new information theory-based analysis of allosteric mechanisms reveals residues that underlie function in the leucine transporter

Nicholas Woodall, University of California, Los Angeles
The positive-inside rule is a local effect

Emilia Ling Wu, University of Kansas
E. coli Outer Membrane and Interactions with OmpLA

Congratulations to all recipients!

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