The MedInProt Protein Science Research Synergy Program (MedInProt) is a unique niche initiative in Hungary which aims to:

  • link different protein science disciplines
  • organize and strengthen their network
  • achieve competitive collaboration
  • catalyze synergy among specialities
  • support recognized researchers' co-operation

The objective of the program, which is financed by the Hungarian Academy of Sciences, is to foster cooperation among a number of universities: the Eötvös Loránd University, the Budapest University of Technology and Economy, the Semmelweis University and the Hungarian Academy of Sciences Research Center for Natural Sciences. 20th May 2014 marked the inaugural conference of the MedInProt Program, whose president is Dr András Perczel.

The first phase of the program (2014 - 2015) was concerned with research into the fields of protein science. We will support some researcher to buy small and medium-sized equipment, and will finance them a measure of computer time.

MedInProt's remit includes the organisation and support of conferences and courses and the establishment of an MSc program in English. In addition, the program will be involved in setting up a troubleshooting hotline, and the purchase and translation of books relating to the field of protein science.



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8. Conference of MedInProt - presented at the conference 2018-04-23

The eighth Conference of the MedInProt Protein Science Research Synergy Program was held on April 21. 2018, at Eötvös Loránd University.

László Nyitray: Resolution revolution

Ferenc Vonderviszt: The revolution of cryo-electron microscopy in determination of biomolecular structures

Max Maletta: How Cryo-EM is changing the Structural Biology landscape for the best

Ágnes Hubert: From protein sample to high-resolution cryo-electron microscopy map

Gergő Gógl: A crystallographer’s perspective on cryo-electron microscopy

Mihály Pósfai: New scientific directions in electron microscopy laboratory

The role of ion channels and pumps in tumor metastasis

Interaction of lysophosphatidic acid with signalling protein domains: affinity, stoichiometry and the site of binding

Role of the scaffold protein Tks4 in cancer cell movement

Setup of inflammation induced permeability measurements by gold nanoparticles and optical biosensor

Pathogenicity and oligomerization of podocin

Nanomechanical tests in the diagnostics of genodermatoses

Studying decision making process between cell death mechanisms: the GSH switch - ferroptosis and autophagy in focus

Investigation of the role of dynamin mediated and mitochondrial pathways in the background of centronuclear myopathy

8. Conference of MedInProt - program 2018-04-12


Cryoem Kep

8. Conference of MedInProt - visiting lecturers 2018-03-29

Mihály Pósfai: New scientific directions in electron microscopy laboratory

Ferenc Vonderviszt: The revolution of cryo-electron microscopy in determination of biomolecular structures

Recent advances in cryo-electronmicroscopy have dramatically reshaped the landscape of structural biology. This technique can be used to determine the three-dimensional structure of biomacromolecules in near native conditions at close to atomic resolution, and has the potential to reveal multiple conformational states related to the dynamic behavior of molecular complexes. Cryo-EM now produces very excit¬ing results addressing a broad range of important biological questions with a level of detail we have never seen before.

Ágnes Hubert: From protein sample to high-resolution cryo-electron microscopy map

Cryo-electron microscopy (cryo-EM), is an increasingly popular technique allowing the examination of a frozen-hydrated specimen in vitreous (non-crystalline) ice. The technique complements X-ray crystallography by revealing structural details without the need for a crystalline specimen. The workflow of single-particle cryo-EM is demonstrated with the case-study of three archaeal protein complexes and the structure of the eukaryotic 26S proteasome.

Gergő Gógl: A crystallographer’s perspective on cryo-electron microscopy

I will discuss the advantages and the potential problems of cryo EM modelling in constrast to the conventional crystallographic structure determination.

László Nyitray: Resolution revolution

The Nobel prize in chemistry in 2017 was awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for developing cryo-electron microscopy as a structural biology method. In the lecture the development of the Method of the Year in 2015 will be briefly described together with the contribution of the Nobel prize winners and further methodological progress in the last couple of years that explains the "resolution revolution".

Max Maletta: How Cryo-EM is changing the Structural Biology landscape for the best

In 2017 R. Henderson, J. Frank and J. Dubochet have been awarded the Nobel prize in Chemistry for having pioneered cryo electron microscopy (Cryo-EM) and Single Particle Analysis (SPA).
During the last few years Cryo-EM and SPA have grown from techniques able to produce low-resolution structures of protein complexes to tools capable of achieving atomic and quasi-atomic resolution for complexes that nobody could solve with any other technique.
This incredible leap forward has been made possible through the introduction and adoption of new tools, in particular direct electron detectors (DED), ultra-stable cryo-microscopes, such as the Titan Krios and the adoption of new SW for automatic data collection and processing.
Cryo-EM benefits of specific advantages, with respect to other structural biology techniques such as NMR and X-ray diffraction:
. Crystallization or isotopic labelling is not needed.
. The amount of sample required is two orders of magnitude lower.
. Different functional conformation of a protein complex may be revealed.
Cryo-EM has proven to be a very useful technique to be integrated with X-ray and NMR for structure-based drug design Thus it is no surprise that many structural biology groups all over the world are seeking access to this technology in order to find answers to their most relevant biological questions. Nevertheless most users that are new to the field of cryo-EM are struggling to overcome the adoption barrier that this technique may pose in terms of: sample preparation and screening, automatic data acquisition and progressive users training.
In this presentation we will present how the fast pace of cryo-EM growth is going to revolutionize the structural biology landscape. In addition, the latest Thermo Fisher Scientific technologies/solutions will be introduced:
- The cryo-EM SPA workflow with the recently introduced electron microscopes Krios G3i and Glacios - today the most economical and efficient Cryo-EM solutions for getting to the 3D structure of protein molecules.
- The recent advances in electron cryo-tomography with the cryo focused-ion-beam, an application for visualization of biological structures in their native, cellular context at the molecular-scale.
- The new development of mED (Micro electron Diffraction): a technology that holds the promise to solve the high resolution 3D structure of proteins crystallized into very small., an interesting cost effective alternative for XFEL.

8. Conference of MedInProt 2018-03-26

We cordially invite you to the 7th MedInProt Conference held at ELTE TTK Eötvös lecture hall on Saturday, April 21, 2018 starting at 9 AM.
Winners of the Synergy VI., VII. and  the Feasibility Study Program shall present their joint research at the conference. In addition, topic covers in cryo-EM Mihály Pósfai and Ferenc Vonderviszt will give lectures.
The conference will end with sweepstakes and poster discussions.
All interested are invited and welcome!

MedInProt film 2018-01-31

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