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Dr Emmanuel FARHI (Synchrotron Soleil)Poster
The newly formed Data Reduction and Analysis group at Synchrotron SOLEIL is responsible for the development and implementation of data analysis software and methods for users of the facility. Rapid and efficient data analysis adds value to the users’ experience and efforts will be made by the group to provide simple and rapid tools for this purpose.
We aim to develop cloud-based...
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Mona Koder Hamid (Master student)Poster
Clays are negatively charged nanoplatelets with a layered silicate structure. It has been observed from small angle X-ray scattering measurements, and coarse-grained molecular dynamics simulations (CG-MD) that clay nanoplatelets are able to form stacks, known as tactoids, in the presence of divalent or multivalent counterions. In this thesis, the interactions between clay nanoplatelets and...
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Kliment Olechnovic (Vilnius University)Oral
Given a molecular structure, it can be represented as a set of atomic balls, each ball having a van der Waals radius corresponding to the atom type. A ball can be assigned a region of space that contains all the points that are closer (or equally close) to that ball than to any other. Such a region is called a Voronoi cell and the partitioning of space into Voronoi cells is called Voronoi...
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David Fernandez (ESRF)Oral
Multispecific antibodies are artificially engineered molecules designed to bind simultaneously to several different antigens. Potential advantages of generating viable multispecific antibodies include the identification of malignant cells coupled with the concurrent recruitment of immune cells and the blocking of complex viral escape mechanisms. The cross-over dual-variable immunoglobulin...
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Ivan Gushchin (Moscow Institute of Physics and Technology)Oral
Recent breakthroughs in X-ray crystallography, Cryo-EM and complementary approaches resulted in elucidation of many new structures of membrane proteins (MPs) and their complexes. Several classes of MPs, such as microbial rhodopsins, rotary ATPase subunits c, or light harvesting complexes 2, form ring-like assemblies with several lipid molecules trapped inside. Whereas the proteins are usually...
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Dr Montserrat Soler Lopez (ESRF)Oral
Neurodegenerative diseases are very complex and a holistic understanding of the relation between structure and function requires the integration of molecular, cellular and systems biology. We applied ‘omic' technologies to generate of a most complete protein interactome associated with Alzheimer’s disease (1). The analysis of this network triggered insights on the mechanisms implicated in the...
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DOMINIQUE MIAS-LUCQUIN (LORIA)Oral
Spread of antibiotic resistance genes by conjugative mechanisms represent a major public health issue. Among the elements involved in these horizontal genes transfers, mechanisms involving integrative and conjugative elements (ICEs) are the most common. The RelSt3 relaxase is a protein that binds to a sequence-specific dsDNA, and to the ssDNA region of a hairpin to cut it prior to its...
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Dr Frederic Cazals (Inria)Oral
Clustering conformations of molecules or molecular assemblies is a
central problem faced in most studies, be they concerned with atomic
models or coarse grain models. This talk will review recent
contributions in this realm.The first one is concerned with the newly designed molecular distance
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RMSDcomb [1]. Given the decomposition of a structure into subdomains,
RMSDcomb provides a weighted... -
Dr Marie Skepö (Div. of Theoretical Chemistry, Dept. of Chemistry, Lund University, Sweden)Oral
Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structure in solution under physiological conditions. Despite this they are functional and participate in the regulation of many biological processes, in which disorder can enable interactions of high specificity coupled with low affinity. Phosphorylation is one of the most abundant types of post-translational...
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Juan Cortés (LAAS-CNRS, Université de Toulouse)Oral
By providing a precise snapshot of the structure of the interface between two protein partners, X-ray crystallography helps identifying point mutations that are likely to strengthen the interaction. However, this technique provides very little information about conformational flexibility, in particular in protein loop fragments. In cases where plasticity may be critical for protein function,...
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Mr Alister Burt (Institut de Biologie Structurale)Oral
Short Abstract
Cryo-electron tomography (cryo-ET) is a technique which allows direct visualisation of vitrified biological samples in 3D. In a framework conceptually similar to single particle analysis in cryo-EM, it is possible to achieve high-resolution (subnanometer and beyond!) insights into macromolecules directly within their cellular context by alignment and averaging of multiple...
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Marc Lensink (CNRS)Oral
Protein-protein interactions play a central role in all biological processes. These processes result from the physical interaction of two or more protein molecules, forming a macromolecular assembly.
The CAPRI (Critical Assessment of PRedicted Interactions) experiment has been a proven catalyst of docking algorithms since its inception almost two decades ago. In recent years, the CAPRI...
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Dr Amin SAGAR (Centre de Biochimie Structurale)Oral
Many biologically important systems are inherently polydisperse e.g. transient protein-protein complexes, oligomerizing proteins or proteins with different co-existing conformations. Such systems are always in an equilibrium of different species and are therefore heterogenous. Importantly, such systems can’t be meaningfully studied in a holistic sense by physically separating the components of...
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Dr Eaazhisai Kandiah (ESRF)Oral
Over the last two decades, single-particle cryo-electron microscopy has emerged as a technique capable of producing routinely near-atomic resolution structures and render to study challenging systems that otherwise defy structural characterization. Recent technical advances in this field have resulted in breakthrough progress in its applicability to various biological macromolecules,...
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Antoine MoniotOral
Protein-RNA interactions are involved in many biological processes like the traduction of messenger RNA to protein, and their modelisation is important to understand them. In particular, non-paired regions of the RNA, i.e., single-stranded RNA (ssRNA), are involved in most of these interactions and are essential for their specificity.
However, ssRNAs are highly flexible and their...
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Dr Pablo ChaconOral
In last the decades, significant progress was made by combining cryo-EM data with high-resolution structures. We review our adventure developing computational fitting techniques to interpret EM data in terms of available atomic structures. We will try to illustrate the power and limitations of our fitting tools with key examples.
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Mathilde Carpentier (ISYEB - MNHN - SU - CNRS - EPHE)Oral
Multiple protein sequence alignments are used daily in bioinformatics to annotate and predict the characteristics of currently mass produced sequences. The quality of their results have been assessed many times and have recahed a plateau. Proteins fold into stable three-dimensional structures with a topology much more conserved than sequence. Consequently, it should be advantageous to use this...
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Adrien Favier (IBS CNRS)Oral
Atomic-resolution structure determination is the key requirement for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination...
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Maria Marcaida (EPFL)Oral
Integrative modeling is a powerful tool to study the structure-function relationship in multi-domain flexible systems. Here we will describe the combination of modelling, solution scattering data and flexible fitting as well as biochemical and biophysical analyses that have been used to define the quaternary structure of DDX21, a human DEAD-box helicase with RNA G-quadruplex resolving...
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Hugo van Ingen (Utrecht University)Oral
Intrinsically disordered proteins (IDPs) are key in wide range of biological processes, from signal-transduction pathways to the protection of genomic integrity. Yet, their unstructure poses a significant challenge for understanding their function at the atomistic level. In our work we aim to decipher the role of the intrinsically disordered acidic domain of APLF (APLFAD) in binding and...
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Mr Albert Miguela Benavides (European Synchrotron Radiation Facility, Grenoble)Poster
The mitochondrial oxidative phosphorylation system (OXPHOS), which includes five protein complexes (CI-V), is the main source of energy in the cell. CI, the largest and first complex, is composed of several protein subunits that are assembled by different assembly factors, such as Acyl-CoA Dehydrogenase Family Member 9 (ACAD9) and Evolutionarily Conserved Signaling Intermediate In Toll Pathway...
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Robert Rambo (Diamond Light Sourcwe)Oral
Understanding how proteins and complexes move in solution remains a major challenge in structural biology. Biological macromolecules are machines that adopt a variety of structural conformations and efficiently exploring this structural space in a comprehensive and meaningful way can not be achieved solely using the solid-state methods cryo-EM and macromolecular crystallography (MX). Small...
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Sergei GRUDININPoster
While crystallography has been providing atomic-resolution structures of biomolecules for over half a century, the real challenge of today’s biophysics is to correlate molecules’ structure and dynamics in solution with their function. Owing to the complexity of the problem, the answer can only be found if multiple sources of information are used simultaneously. I will present a set of tools...
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Lina ALFERKH (University of Paris Descartes (University of Paris) - Cibles Thérapeutiques et Concéption de Médicaments (CiTCoM) UMR 8038 CNRS)Poster
Since the conformation of RiboNucleic Acids (RNA) is a key for its function, experimental techniques at different levels of resolution are implemented to determine its structure. Because of the flexibility and the large size of certain RNAs, their structure cannot be determined through high resolution experiments, such as nuclear magnetic resonance (NMR) and X-Ray crystallography. It is...
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Dr Massimiliano Bonomi (Institut Pasteur - CNRS)Oral
Cryo-electron microscopy is rapidly emerging as a powerful technique to determine the structures of complex macromolecular systems elusive to other techniques. Since many of these systems are highly dynamical, characterising also their movements is a crucial step to unravel their biological functions. In this talk, I will present an integrative modelling approach to simultaneously determine...
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Amanda ERIKSSON SKOGPoster
Histatin 5 (Hst5) is a histidine-rich, 24 amino acid protein, classified as an intrinsically disordered protein (IDP). It contains 7 histidines, an amino acid sensitive to charge regulation. The histidines can titrate and gain a positive charge, making the protein highly cationic. Hst5 is a salivary protein found to play a crucial role in fungicidal activity, and its activity to inhibit the...
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Matthew BOWLER (EMBL)Oral
Pathogens often evolve methods of modulating host cell signalling pathways in order to promote their growth and persistence in the infected cell. One of the most efficient methods to interact with host signalling proteins is the use of intrinsically disordered proteins combined with short linear motifs, as the evolutionary timescales involved are shorter than those required for globular...
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Dr Francois FERRON (Architecture et Fonction des Macromolécules Biologiques, AFMB - CNRS)Oral
In the recent years a massive amount of raw viral genomic data has been produced and released in sequenced databases, leading to the paradoxical situation of generating the Domain of Unknown Function (DUF), the number one domain in knowledge databases. Together with bio-informatics prediction, the knowledge of the three-dimensional structures of DUF proteins is the key to unveil the full...
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Dr Montserrat Soler-López (European Synchrotron Radiation Facility)Poster
The mitochondrial respiratory complex I is the largest of the large mitochondrial respiratory complexes, being roughly 1 MDa in size. Consequently, its assembly process is extremely complicated, requiring multiple assembly factors. Two such factors, acyl-CoA dehydrogenase 9 (ACAD9) and the evolutionarily conserved signalling intermediate in the Toll pathway (ECSIT) appear to act in a complex...
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Didier Devaurs (INRIA)Poster
Experimentally observing and/or computationally modeling large proteins and macromolecular complexes remain critical challenges for structural biology. Hydrogen-exchange monitoring is cheap and easy to carry out, but cannot produce structural models because of its low resolution. To mitigate this issue, one side of our coupled approach consists of developing computational methods to complement...
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Prof. Samuela PasqualiOral
Electrostatic interactions play a pivotal role in many (bio)molecular association processes. The molecular
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organization and function in biological systems are largely determined by these interactions from pure
Coulombic contributions to more peculiar mesoscopic forces due to ion-ion correlation and proton
fluctuations. By means of constant-pH Monte Carlo simulations based on a fast... -
Dr Agnieszka Karczynska (Univ. Grenoble Alpes, Inria, CNRS, Grenoble INP, LJK, 38000 Grenoble, France)Poster
Prediction of protein structures is one of the most important problems of current structural bioinformatics. Many proteins in living organisms form multimeric structures or are involved in the complexes with other biomacromolecules, such as other proteins or small ligands. Prediction of protein structure in the monomeric state is already very challenging and therefore the structures of their...
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martin blackledgeOral
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