Archive by category: Upcoming Events

Mini-Symposium on Computational Approaches on May 8th

Wednesday May 8th 2013, 9:00 AM to 5:00 PM
Gordon Center for Integrative Science, room W301/303
University of Chicago (directions)

Note: the Computational Modeling Core is also hosting a workshop specifically dedicated to membrane protein modeling at the University of Chicago on May 7th. Click here to learn more and register »

Force field and atomic models

9:00 Lei Huang: Advances in automatic force field optimization
9:15 Christopher Mayne: Force Field Toolkit (FFTK)
9:30 Sunhwan Jo: Recent developments in CHARMM-GUI and CHARMM-GUI Membrane Builder
9:45 Wei Han: Further development of a mixed all-atom/united-atom models for simulation of peptide folding, aggregation and proteins in membrane
10:00 George Khelashvili: Protein-membrane coupling and the calculation of the bending rigidity of multi-component lipid membranes
10:15 Brigitte Ziervogel: Simulation of membrane systems with asymmetrical conditions
10:30 Josh Vermaas: Developing novel in silico solvents with optimized properties mimicking membrane models
10:45 Break
11:00 Niklaus Johner: Membrane proteins in the cubic phase lipid environment – insights into in meso crystallization environments
11:15 Yifei Qi: Quantifying the Drive-Response Relationships between Residues in Protein Folding

Structural modeling with low-resolution data

11:30 Aashish Adhikari: LBT loop modeling protocols
11:45 Shahid Islam: Structural refinement using ESR/DEER histogram data
12:00 Fatemeh Khalili: Structural refinement using low-resolution LRET data
12:15 Lunch
1:30 Huan Rui: Probing Human Growth Hormone Receptor Structure Using Computational Simulations and NMR spectroscopy
1:45 Abhishek Singharoy: xMDFF – Molecular Dynamics Flexible Fitting of Low Resolution X-ray Structures
2:00 Hang Yu: Membrane Sculpting by F-BAR Domains by Molecular Dynamics Simulation

Transition pathways

2:15 Avisek Das: A simple method to determine conformational transition pathways based on a two-state anisotropic elastic network model
2:30 Mert Gur: Global Motions of Proteins Observed in Micro- to Milliseconds Simulations Concur with Anisotropic Network Model Predictions
2:45 Wen Ma: Study of conformational transitions of hexameric motors using the string method
3:00 Break
3:15 Mahmoud Moradi: Application of collective variables to describe large-scale conformational changes of membrane transporters
3:30 Zhe Wu: A New Hypothesis for the Mechanism of Synaptotagmin I in Synaptic Neurotransmitter Release
3:45 Po-Chao Wen: The impact of the lipid environment on gating of KcsA

Spectroscopy

4:00 Josh Carr: Introduction to computational analysis of 2D-IR spectroscopy

Conclusion

4:15 Roundtable discussion

Workshop on Membrane Protein Production on May 8th

Wednesday May 8th 2013, 2:00 PM to 5:00 PM
Knapp Center for Biomedical Discovery, room 3200
University of Chicago (directions)


This expression test gel was produced by Bea Hoffman from Volker Dötsch‘s lab

Join us for an afternoon to discuss topics on membrane protein production and modification.  Topics will include cellular and cell-free production of membrane proteins, reconstitution, incorporation of unnatural amino acids, single antigen binder technologies, and chemistry of protein modification and nitroxide spin labels.

Click here to register

Schedule

2:00    Brandy Verhalen, Vanderbilt University, and Yelena Peskova, University of Virginia: Expression in eukaryotic cells and reconstitution into nanodiscs.

2:20    Shohei Koide, University of Chicago: Use of designed binding proteins for structural and functional studies

2:40    Ray Hulse, University of Chicago: Strategies for NMR sample preparation

3:00    Edith Buchinger, Goethe University: Cell-free protein synthesis for NMR

3:20    Break

3:40    Stephen Pless, University of Iowa: Use of nonsense suppressors in ooctyes

4:00    Lilia Leisle, University of Iowa: Selection of tRNA synthetases for in vivo incorporation of unnatural amino acid

4:20    Andrzej Rajca, University of Nebraska: Next generation nitroxide spin labels

4:40    Discussion

5:00    End of workshop

Membrane Protein Modeling workshop to take place at the University of Chicago on May 7th

During the week of the Membrane Protein Structural Dynamics Consortium (MPSDC)’s Annual Meeting, a workshop specifically dedicated to Membrane Protein Modeling will be held at the University of Chicago on Tuesday, May 7th. This Workshop is designed to provide an introduction to the most important computational tools and techniques used in molecular dynamics simulations of membrane proteins, including utilization of the programs NAMD and VMD, as well as the CHARMM-GUI Membrane Builder. We will also cover the use of force field parameterization tools. The workshop will include a practical “hands-on” session.

The Workshop is co-organized by the Computational Modeling Core (CMC) of the MPSDC and the Theoretical and Computational Biophysics Group (TCBG) of the University of Illinois at Urbana-Champaign.

Register for the CMC Membrane Protein Workshop (required) »



Last year’s CMC Workshop, also held at the University of Chicago.

The next MPSDC annual meeting will be May 9-10, 2013. Save the date!

Save the date for the next annual meeting scheduled to be held May 9-10, 2013. The location will be here in Chicago, and the venue will be announced soon!

In May 2012 the Membrane Protein Structural Dynamics Consortium (MPSDC) held its first Frontiers in Membrane Protein Structural Dynamics conference at the Gleacher Center in Chicigao. This year our annual meeting will provide similar opportunities for group conversation and collaboration between participants. We hope you will join us!

Participants gathered on the stairs at the Gleacher Center for a group photo.

First Frontiers in Membrane Protein Structural Dynamics Conference was a success



Dorothee Kern, Brandeis University and External Advisory Committee Member

On May 3rd and 4th, the Membrane Protein Structural Dynamics Consortium (MPSDC) held its first Frontiers in Membrane Protein Structural Dynamics conference. The conference consisted of scientific sessions and poster presentations, and featured both Consortium members and external invitees. Attendance was open to the public took place within the context of our 3rd Annual MPSDC Meeting, where all members, NIH representatives and our External Advisory Committee participated. Prior to the conference, the MPSDC’s Computational Modeling Core hosted a NAMD/VMD workshop and a mini-symposium concerning the latest advances in membrane protein modeling.



Miguel Holmgren, NINDS and collaborator in Bridge 1: Conformational Transitions in P-class ATPases

Both the conference and CMC events were very well attended and enabled extensive conversations surrounding the topic of cutting edge advances and scientific methods in the field of membrane protein dynamics, as well as ways to resolve current roadblocks. The conference was able to hit a high note in bringing together the issues and ideas most relevant to the key goals of the consortium both in the present and in the future. Chris Ahern of the University of British Columbia and MPSDC Associate Member noted afterwards that it was probably one of the best meetings he’s been to, “primarily because of the quality of the science that’s being done, as well as the excitement and eagerness of people to cooperate.”



José Faraldo-Gómez, Max Planck Institute for Biophysics and MPSDC Associate Member

In the afternoon, two discussion panels were held, which themselves are in the spirit of much of the broader conversations that took place at the conference as a whole. The first panel, “Finding a common language: linking experiment and computation” was chaired by Hassane Mchaourab, and included Benoît Roux, Martin Zanni, Ivet Bahar, Dorothee Kern, and Emad Tajkhorshid as participants.



Chris Ahern, University of British Columbia and MPSDC Associate Member

The second panel was titled “Breaking the barriers of membrane protein expression and labeling” and was moderated by Robert Nakamoto. The panel included Chris Ahern, Jim Bowie, Volker Dötsch and Shohei Koide. Discussion focused on three topics: the optimal nitroxide spin probe for monitoring protein dynamics and DEER distance measurements, how to incorporate such a probe into the protein targets, and cell free synthesis of target proteins. The optimal nitroxide spin probe would be connected to the backbone by only a β carbon. Such a label can be introduced using chemical synthesis, but because most of our proteins are too large, methods for bio-incorporation of unnatural amino acid are preferred. Cell free biosynthesis systems such as those developed in the laboratory of Volker Dötsch, Goethe University, and Chris Ahern, University of British Columbia, may provide the best approaches. The Protein Core labs will explore methods for charging the non-sense tRNA by evolved tRNA synthetases or a ribozyme using technologies called the Flexizyme developed by Soga and co-workers at Tokyo University. The acylated TAG tRNA charged with the spin probe is simply added to the cell free synthesis mix. Another issue is the lability of nitoxides to reduction by ascorbic acid. We will test a variety of nitroxide spin probes, which have been reported to be relatively insensitive to reduction. Finally, we discussed specific placement of labels using synthetic binders. In particular, the synthetic 10FN3 binders, or monobodies (~93 aa, derived from a type III fibronectin domain), can mediate specific labeling of a protein and effectively attach a label or cargo to the protein target with high affinity and stability.

We’d like to thank all who attended and partook in the discussions. By all accounts, it is hard to think of a better outcome for the conference and accompanying events, and we look forward to hosting another meeting in two years.

Below is a gallery displaying photos of the conference. You can either scroll through the photos here or visit the set on Flickr. We’ve also made available several brief audio interviews with attendees of the conference, to be found in the margins of the body of this post.

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