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Dynamics of Biological Macromolecules

4–6 Jun 2018
Skissernas Museum
Europe/Stockholm timezone

Session

Dynamics of Intrinsically Disordered Proteins

DIDP
4 Jun 2018, 13:15
Skissernas Museum

Skissernas Museum

Finngatan 2 223 62 Lund Sweden

Presentation materials

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  1. 67. KEYNOTE 1 - Dynamics of intrinsically unfolded and partially folded proteins: Insights gained by quasielastic neutron scattering
    Dr Andreas Stadler (Forschungszentrum Jülich)
    04/06/2018, 13:15
    Dynamics of intrinsically disordered proteins
    Oral presentation

    A general property of disordered proteins is their structural expansion that results in a high macromolecular flexibility. Quasielastic incoherent neutron scattering (QENS) is a well-suited experimental method to study protein dynamics from the picosecond to several nanoseconds and in the Ångström length-scale. In QENS experiments of protein solutions hydrogens act as reporters for the motions...

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  2. 47. Contributed talk 1 - Exploring protein association pathways with time-resolved SAXS and SANS
    Dr Wojciech Potrzebowski (European Spallation Source)
    04/06/2018, 13:55
    Dynamics of intrinsically disordered proteins
    Oral presentation

    Protein performs its biological functions by interacting with other proteins. Protein complexes, which are formed as a result of these interactions, consist of two or more components that associate along specific pathways - protein association pathways. The association pathway from monomer to oligomer is critical in a range of biological processes and thus it is of a vital importance to...

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  3. 50. Contributed talk 2 - Structural characterization of intrinsically disordered protein micelles
    Ellen Rieloff
    04/06/2018, 14:15
    Dynamics of intrinsically disordered proteins
    Oral presentation

    To obtain a molecular understanding of IDPs, a combined approach of experiments and simulations is useful. Recently we have shown that a coarse-grained model based on the primitive model, that has been used for modelling polyelectrolytes for over 30 years, works well for a range of IDPs where electrostatics governs the intra- and intermolecular interactions [1]. However, some IDPs have the...

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  4. 42. KEYNOTE 2 - Dynamics and interactions of disordered proteins from single-molecule spectroscopy
    Prof. Benjamin Schuler (University of Zurich)
    04/06/2018, 14:35
    Dynamics of intrinsically disordered proteins
    Oral presentation

    Proteins are the most versatile constituents of the molecular machinery of life, and it is becoming increasingly clear that many of them perform essential functions even though they lack a well-defined folded structure. Single-molecule spectroscopy and fluorescence correlation spectroscopy provide an opportunity for investigating the molecular dynamics of these intrinsically disordered...

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  5. 52. KEYNOTE 3 - Characterization of intrinsically disordered proteins and their dynamic complexes by NMR spectroscopy
    Dr Malene R. Jensen (Institut de Biologie Structurale, Grenoble)
    04/06/2018, 15:45
    Dynamics of intrinsically disordered proteins
    Oral presentation

    Over the last two decades, the classical structure-function paradigm has gradually been revisited with the discovery and the increasingly recognized importance of intrinsically disordered proteins (IDPs). IDPs do not rely on a well-defined three-dimensional structure to be functional, but rather exploit their intrinsic conformational dynamics for carrying out a wide range of biological...

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  6. 69. KEYNOTE 4 - Comparing molecular simulations with NMR and SAXS measurements: A cautionary tale
    Prof. Kresten Lindorff-Larsen (University of Copenhagen)
    04/06/2018, 16:25
    Dynamics of intrinsically disordered proteins
    Oral presentation

    The degree of compaction of the polypeptide chain is a property of key importance in intrinsically disordered proteins. Experimentally, compaction is often measured either by NMR (as the hydrodynamic radius) or SAXS (as the radius of gyration), and more detailed information may also be obtained by NMR paramagnetic relaxation enhancement measurements. A more detailed, atomic-level description...

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  7. 49. A computational and experimental investigation of the structural properties of Keif, the intrinsically disordered N-terminus part of MgtA
    Ms Stephanie Jephthah (Lund University)
    Dynamics of intrinsically disordered proteins
    Poster

    A recent study by Subramani et al. (eLife, 2016) implied that the N-terminus of the magnesium transporter A (MgtA) protein (from hereon called Keif) is intrinsically disordered, but the advantage of this disordered feature to the function of the protein is still unknown. Thus, in this study, the structure of the Keif peptide part have been investigated by using both atomisic molecular...

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  8. 15. Contributed Talk 1: Exploring protein association pathways with time-resolved SAXS and SANS
    Wojciech Potrzebowski (European Spallation Source, ERIC)
    Dynamics of intrinsically disordered proteins
    Oral presentation
  9. 16. Contributed Talk 2: Structural characterization of intrinsically disordered protein micelles
    Ellen Rieloff
    Dynamics of intrinsically disordered proteins
    Oral presentation
  10. 20. Contributed Talk 4
    Dynamics of intrinsically disordered proteins
    Oral presentation
  11. 19. Contrinuted Talk 3: Efficient Prediction of Macromolecular Flexibility and its Applications to Small-Angle Scattering
    Sergei Grudinin (Inria / CNRS)
    Dynamics of intrinsically disordered proteins
    Oral presentation
  12. 14. KEYNOTE 1 - Dynamics of intrinsically unfolded and partially folded proteins: Insights gained by quasielastic neutron scattering
    Dr Andreas Stadler (Forschungszentrum Jülich)
    Dynamics of intrinsically disordered proteins
  13. 17. KEYNOTE 2 - Dynamics and interactions of disordered proteins from single-molecule spectroscopy
    Prof. Ben Schuler (University of Zürich)
    Dynamics of intrinsically disordered proteins
  14. 18. KEYNOTE 3 - Visualising the structure, dynamics and interaction mechanisms of intrinsically disordered proteins by NMR spectroscopy
    Dr Malene Ringkjøbing Jensen (University of Grenoble Alpes, CNRS)
    Dynamics of intrinsically disordered proteins
  15. 24. KEYNOTE 4 - Comparing molecular simulations with NMR and SAXS measurements: A cautionary tale
    Prof. Kresten Lindorff-Larsen (University of Copenhagen)
    Dynamics of intrinsically disordered proteins
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