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CCPN / CCPBioSim joint conference 2016

25th-28th July 2016, University of Derby, Buxton

Address for the conference site:

The Devonshire Dome,
1 Devonshire Road,
Buxton, Derbyshire, SK17 6RY

Travel information. Note that there is limited parking at the conference site and all parking should be done on the nearby streets unless you have a requirement to park at the conference site. Accommodation is in the High Peak Halls.  Towels are provided in the accommodation but not toiletries like soap and toothpaste.

People arriving Sunday: High Peak Halls is open from 2 PM

People arriving Monday: High Peak Halls is open 11 AM - 12 noon and then again after the session

The yearly CCPN meeting aims to present current best practice for all aspects of macromolecular NMR and is particularly aimed at PhD students and Post-docs, mainly in the UK Biomolecular NMR community.  The speakers will discuss in detail the pros and cons of the different approaches they they are using.  Through discussion, we hope to come up with new ideas as to how future NMR structural projects might best be tackled.

This year the conference is joint with CCP-BioSim (the Collaborative Computational Project for Biomolecular Simulation) and there will be two sessions on this aspect.

The conference starts with registration and a buffet lunch on Monday 25 July 2016, and the first talks that day are after lunch. The conference finishes at 12.45 on Thursday 28 July.

This year's programme will include the follow sessions:

Session 1: The interface between NMR and Modelling

  • Benjamin Bardiaux (Institut Pasteur, Paris)
    Accurate and efficient structure calculation from solution and solid-state NMR data
  • Tiago Cordeiro (Centre de Biochimie Structurale de Montpellier, CNRS, Montpellier)
    Disentangling flexible, transient and multivalent macromolecular assemblies
  • Markus Weingarth (Utrecht University)
    Peptide and Protein assembly by solid-state NMR and MD simulations
  • Simon Olsson (Freie Universität Berlin)
    Combining molecular simulations and NMR: from structure ensembles to molecular kinetics

Session 2 : Complexes and transient interactions

  • Irene Diaz Moreno (IBVF, Seville)
    How Molecules Form Transient Complexes in Photosynthesis and Respiration

  • Mikaël Feracci (University of Leicester)
    Structural basis of RNA recognition and dimerization by the STAR proteins
    T-STAR and Sam68

  • Rivka Isaacson (King's College London)

    Transient interactions as decision points in protein quality control

  • Enrico Luchinat (CERM, Florence)
    Protein folding and maturation in mammalian cells by NMR

 

Session 3: Biomolecular Dynamics

  • Julien Michel (University of Edinburgh)
  • Biomolecular simulations: challenges and opportunities for synergies with biophysical measurements of protein-ligand interactions

  • Ulrich Zachariae (University of Dundee)
    Ion movement in membrane proteins under voltage: Functional mechanisms of ion channels and beyond
  • Andrea Cavalli (University of Bologna / IIT Drug Discovery)
    Thermodynamics and kinetics of drug-target binding through molecular simulations
  • Edina Rosta (King's College London)
    Dynamics and Reaction Mechanism of Phosphate Catalytic Enzymes



Session 4 : NMR and alternative techniques

  • Frédéric Allain (ETH Zurich)
    Structures of protein RNA complexes using NMR, EPR and Mass-spectrometry
  • Jason Schnell (University of Oxford)
    Molecular mechanisms in stabilising ER membrane tubules by   DP1/Reticulon proteins
  • Michael Sattler (Technical University of Munich)
    Studying conformational dynamics and molecular recognition using integrated structural biology in solution
  • Joern Werner (University of Southampton)
    When the whole is more than its parts: Molecular mechanisms of eukaryotic elongation factor 2 kinase (eEF2K) activation



Session 5 : Prediction of observables

  • Phil Biggin (University of Oxford)
    MD predictions and electrophysiology give powerful insight into ionotropic glutamate receptor function
  • Lars Bratholm (University of Copenhagen)
    Protein Structure Refinement Using Quantum Mechanics-Derived Chemical Shift Prediction
  • Wouter Boomsma (University of Copenhagen)
    Molecular simulations driven by NMR chemical shifts: the nature of the bias
  • Marieke Schor (University of Edinburgh)
    Interfacial adsorption of proteins - insights from experiments and multiscale modelling