PIER Graduate Week 2016

10 Oct 2016, 08:00 → 13 Oct 2016, 18:00 Europe/Berlin

SemRoom I-IV, CFEL, Bldg. 99 (Bahrenfeld Campus ( DESY))

Welcome to the PIER Graduate Week 2016, an interdisciplinary lecture and workshop week for PhD students. The PIER Graduate Week offers a wide range of introductory and focus courses in the PIER research fields of Particle & Astroparticle Physics, Nanoscience, Photon Science, Infection & Structural Biology. It aims at PhD students, MSc students, postdoctoral researchers and other interested scientists.

The graduate week's main objective is to introduce PhD students to neighbouring research fields, and to offer stimulating specialists' lectures from both national and international experts, thereby broadening the interdisciplinary understanding and exchange among young scientists on Bahrenfeld campus. A scientific colloquium, an industry lecture and a number of research and career skills workshops complement the programme. During the graduate week, joint coffee breaks, lunches and get-togethers provide great opportunities for informal discussions, exchange of ideas, socialising and fun.

Introductory and focus courses
Each course is a consecutive four-day series of mini lectures. The introductory courses are designed for doctoral candidates who would like to learn more about a related research field, while the focus courses are for those interested in in-depth sessions in their own area of expertise.

Scientific colloquium
The scientific colloquium is a talk given by a high profile speaker, who provides an overview of one of the research areas within the PIER research fields. This year, we have invited Prof. Dieter Luest, Max-Planck-Institute for Physics and Ludwig-Maximilians-Universität, Munich, who will talk about "Quantum Aspects of Black Holes".

Industry talk
On Tuesday, 11 October, Dr. Sven Klussmann, Chief Scientific Officer of NOXXON Pharma AG, Berlin, will give a talk about his inspiring career from a PhD student to a successful science start-up founder and co-owner of a well-established stock corporation. NOXXON Pharma is a biotechnology company focusing on cancer treatment. 

Research and career skills workshops
These complementary workshops combine short lectures with practical exercises and homework. Please note: The places for the workshops are limited.

Speakers
Gleb Arutyunov (Hamburg), Tobias Brandes (Berlin), Andrew Cleland (Chicago), Karsten Danzmann (Hannover, tbc), Monika Fleischer (Tübingen), Niek van Hulst (Barcelona), Sven Klussmann (Berlin), Peter Kolb (Marburg), Jochen Küpper (Hamburg), Dieter Lüst (Munich), Henning Moritz (Hamburg), Angel Rubio (Hamburg), Kazuki Sakurai (Durham, UK), Henning Tidow (Hamburg), Sebastian Trippel (Hamburg), Karel Vyborny (Prague), Gerhard Wolber (Berlin)

Local organising committee
Robert Blick (Nanosciences), Jochen Küpper (Photon Science), Jan Louis (Particle and Astroparticle Physics), Markus Perbandt (Infection and Structural Biology), Robin Santra (speaker of the PIER Helmholtz Graduate School), Mirko Siemssen (PIER Helmholtz Graduate School), Matthias Kreuzeder (DESY)

Poster Poster_PIER_GradWeek_2016.pdf

Programme Programme_PIER_GradWeek_2016.pdf

Monday 10 October

A1: Introductory course Particle and Astroparticle Physics: tba

A2: Introductory course Infection and Structural Biology, Prof. Dr. Henning Tidow (Institut für Biochemie und Molekularbiologie, Hamburg): Proteins - Structure and Function

'Proteins - Structure and Function'
Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, transport and store other molecules such as oxygen, provide mechanical support and immune protection, generate movement, transmit nerve impulses, and control growth and differentiation.

As the function of proteins is determined by their structure, structural biology is the key to understand the structure-function relationship of proteins. In my lecture, I will briefly introduce basic principles that determine the structure of proteins as well as experimental techniques that can be used to study protein structure. Selected examples will be used to illustrate the role of protein dynamics, conformational changes and protein-protein interactions in various physiological processes.

In the second part of the lecture series I will focus on membrane proteins and explain their special characteristics. Structure and function of different classes of integral membrane proteins will be introduced and discussed in relation to the biochemical/physiological processes they are involved in.

10:30 Coffee Break

B1: Introductory course Photon Science, Henning Moritz (Universität Hamburg): Making and probing ultracold atoms: BEC, Fermionic superfluidity and optical lattices

In this course, I will introduce non-specialists to the field of cold atoms. After a short overview over cooling techniques, I will introduce the phenomenon of Bose-Einstein condensation and some milestone results obtained with them. Then we will turn to the field of Fermi gases, talking about the unique possibilities to tune the interactions. This tuneability enables the quantum simulation of strongly correlated superfluidity in the crossover from Bardeen-Cooper-Schrieffer superfluidity to the Bose-Einstein condensation of pairs. Finally we will study the physics of ultracold bosons and fermions in periodic potentials.

1 Slides

B2: Introductory course Nanoscience, Karel Vyborny (Institute of Physics of the Czech Academy of Sciences, Prag): Introduction to selected phenomena of quantum transport

Introduction to selected phenomena of quantum transport
Electric conductivity - a prime example of a transport phenomenon - can be described classically in many cases. Electrons are thought of as point-like particles with definite velocity, accelerated by electric field which carry electric current. Quantum-mechanical view where electrons are considered waves is often leading to practically the same conclusions as the classical one. This course deals with a subjectively selected group of phenomena where the two pictures differ and genuine consequences of quantum mechanics become apparent. For example, the measured transversal resistivity in the Quantum Hall Effect exhibits steps quantized in the units of h/e^2 whereas it is strictly linear (without steps) in the applied magnetic field in its classical version. Given that the quantum mechanics describes microscopical objects (such as individual atoms), it is no surprise that many of these phenomena occur in devices with nanometre size and/or reduced dimensionality.
Syllabus: (1) Classical vs quantum transport. Basics of quantum mechanics. Heterostructures. (2) Conductance and thermopower quantisation in 1D. Tunneling through a quantum dot. (3) Aharonov-Bohm effect. Quantum Hall Effects. (4) Spintronics at nanoscale: magnetic tunneling junctions,
spin-orbit torques and ferromagnetic resonance.

12:30 Lunch break

C1: Focus course Photon Science: tba

C2: Focus course Infection and Structural Biology, Dr. Peter Kolb (Philipps Universität Marburg): Structure based drug design I

In these lectures, I will introduce the basic concepts and possibilities of protein structure-based drug design (SBDD). A prototypical approach in this area is docking. Docking and related methods are based on force fields, describing molecular interactions with biophysical or empirical terms. In the absence of an experimentally determined protein structure, such force fields can also be used to calculate 3D structures through homology modeling. The combination of all techniques constitutes a powerful tool set that can be employed to search for ligands with tailored properties.
I will also highlight key lessons learned from docking multi-million compound libraries to different G protein-coupled receptors (GPCRs), the protein family most frequently targeted by present-day drugs. The most prominent example is the first unbiased screen we did with the β2-adrenergic receptor, which produced six novel binders – some of them with chemotypes previously undescribed for this target – and a most potent compound with an affinity of 9 nM [1]. Further examples include the chemokine receptors CXCR3 and CXCR4, where we identified potent ligands with tailored selectivity profiles with high hit rates [2]. The malleability of GPCRs seems to make multi-conformation screenings a good strategy, as we have shown for the A1 subtype of the adenosine receptors [3]. At the low-throughput end, I will talk about the docking-based in-depth analysis of four ligands of the orexin receptor subtype 2 [4]. The challenge in this system were the unusual binding mode of the crystallographic ligand as well as the comparative scarcity of binding site features. These learnings have now been translated into additional ligands of this highly investigated system.

References
[1] Kolb P, Rosenbaum DM, Irwin JJ, Fung JJ, Kobilka BK, et al. Structure-based discovery of β2-adrenergic receptor ligands. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 6843–6848.

[2] Schmidt D, Bernat V, Brox R, Tschammer N, and Kolb P. Identifying modulators of CXC receptors 3 and 4 with tailored selectivity using multi-target docking. ACS Chem. Biol. 10 (2015), 715–724.
[3] Kolb P, Phan K, Gao ZG, Marko AC, Sˇali A, et al. Limits of ligand selectivity from docking to models: In silico screening for A1 adenosine receptor antagonists. PLoS ONE 7 (2012), e49 910.

[4] Yin J, Mobarec JC, Kolb P, and Rosenbaum DM. Crystal structure of the human OX2 orexin receptor bound to the insomnia drug suvorexant. Nature 519 (2015), 247–250.

C3: Soft skills I (group A)

C4: Soft skills II (group A)

15:30 Coffee break

D1: Focus course Particle and Astroparticle Physics: tba

D2: Focus course Nanoscience: Niek van Hulst (Institute of Photonic Sciences, Barcelona): Light at the nanoscale: ultrafast meets ultrasmall

D3: Soft skills I (group B)

D4: Soft skills II (group B)

17:30 Coffee Break

Scientific colloqium: tba

Tuesday 11 October

A1: Introductory course Particle and Astroparticle Physics: tba

A2: Introductory course Infection and Structural Biology, Prof. Dr. Henning Tidow (Institut für Biochemie und Molekularbiologie, Hamburg): Proteins - Structure and Function

'Proteins - Structure and Function'
Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, transport and store other molecules such as oxygen, provide mechanical support and immune protection, generate movement, transmit nerve impulses, and control growth and differentiation.

As the function of proteins is determined by their structure, structural biology is the key to understand the structure-function relationship of proteins. In my lecture, I will briefly introduce basic principles that determine the structure of proteins as well as experimental techniques that can be used to study protein structure. Selected examples will be used to illustrate the role of protein dynamics, conformational changes and protein-protein interactions in various physiological processes.

In the second part of the lecture series I will focus on membrane proteins and explain their special characteristics. Structure and function of different classes of integral membrane proteins will be introduced and discussed in relation to the biochemical/physiological processes they are involved in.

10:30 Coffee break

B1: Introductory course Photon Science, Henning Moritz (Universität Hamburg): Making and probing ultracold atoms: BEC, Fermionic superfluidity and optical lattices

In this course, I will introduce non-specialists to the field of cold atoms. After a short overview over cooling techniques, I will introduce the phenomenon of Bose-Einstein condensation and some milestone results obtained with them. Then we will turn to the field of Fermi gases, talking about the unique possibilities to tune the interactions. This tuneability enables the quantum simulation of strongly correlated superfluidity in the crossover from Bardeen-Cooper-Schrieffer superfluidity to the Bose-Einstein condensation of pairs. Finally we will study the physics of ultracold bosons and fermions in periodic potentials.

B2: Introductory course Nanosciences, Karel Vyborny (Institute of Physics of the Czech Academy of Sciences, Prag): Introduction to selected phenomena of quantum transport

Introduction to selected phenomena of quantum transport
Electric conductivity - a prime example of a transport phenomenon - can be described classically in many cases. Electrons are thought of as point-like particles with definite velocity, accelerated by electric field which carry electric current. Quantum-mechanical view where electrons are considered waves is often leading to practically the same conclusions as the classical one. This course deals with a subjectively selected group of phenomena where the two pictures differ and genuine consequences of quantum mechanics become apparent. For example, the measured transversal resistivity in the Quantum Hall Effect exhibits steps quantized in the units of h/e^2 whereas it is strictly linear (without steps) in the applied magnetic field in its classical version. Given that the quantum mechanics describes microscopical objects (such as individual atoms), it is no surprise that many of these phenomena occur in devices with nanometre size and/or reduced dimensionality.
Syllabus: (1) Classical vs quantum transport. Basics of quantum mechanics. Heterostructures. (2) Conductance and thermopower quantisation in 1D. Tunneling through a quantum dot. (3) Aharonov-Bohm effect. Quantum Hall Effects. (4) Spintronics at nanoscale: magnetic tunneling junctions,
spin-orbit torques and ferromagnetic resonance.

12:30 Lunch break

C1: Focus course Photon Science: tba

C2: Focus course Infection and Structural Biology, Dr. Peter Kolb (Philipps Universität Marburg): Structure based drug design I

In these lectures, I will introduce the basic concepts and possibilities of protein structure-based drug design (SBDD). A prototypical approach in this area is docking. Docking and related methods are based on force fields, describing molecular interactions with biophysical or empirical terms. In the absence of an experimentally determined protein structure, such force fields can also be used to calculate 3D structures through homology modeling. The combination of all techniques constitutes a powerful tool set that can be employed to search for ligands with tailored properties.
I will also highlight key lessons learned from docking multi-million compound libraries to different G protein-coupled receptors (GPCRs), the protein family most frequently targeted by present-day drugs. The most prominent example is the first unbiased screen we did with the β2-adrenergic receptor, which produced six novel binders – some of them with chemotypes previously undescribed for this target – and a most potent compound with an affinity of 9 nM [1]. Further examples include the chemokine receptors CXCR3 and CXCR4, where we identified potent ligands with tailored selectivity profiles with high hit rates [2]. The malleability of GPCRs seems to make multi-conformation screenings a good strategy, as we have shown for the A1 subtype of the adenosine receptors [3]. At the low-throughput end, I will talk about the docking-based in-depth analysis of four ligands of the orexin receptor subtype 2 [4]. The challenge in this system were the unusual binding mode of the crystallographic ligand as well as the comparative scarcity of binding site features. These learnings have now been translated into additional ligands of this highly investigated system.

References
[1] Kolb P, Rosenbaum DM, Irwin JJ, Fung JJ, Kobilka BK, et al. Structure-based discovery of β2-adrenergic receptor ligands. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 6843–6848.

[2] Schmidt D, Bernat V, Brox R, Tschammer N, and Kolb P. Identifying modulators of CXC receptors 3 and 4 with tailored selectivity using multi-target docking. ACS Chem. Biol. 10 (2015), 715–724.
[3] Kolb P, Phan K, Gao ZG, Marko AC, Sˇali A, et al. Limits of ligand selectivity from docking to models: In silico screening for A1 adenosine receptor antagonists. PLoS ONE 7 (2012), e49 910.

[4] Yin J, Mobarec JC, Kolb P, and Rosenbaum DM. Crystal structure of the human OX2 orexin receptor bound to the insomnia drug suvorexant. Nature 519 (2015), 247–250.

C3: Soft skills I (group A)

C4: Soft skills II (group A)

15:30 Coffee break

D1: Focus course Particle and Astroparticle Physics: tba

D2: Focus course Nanosciences, Monika Fleischer (Eberhard Karls Universität Tübingen): Nanofabrication and spectroscopy of optical antennas

D3: Soft skills I (group B)

D4: Soft skills II (group B)

17:30 Coffee break

Industry talk & reception, Dr. Sven Klussmann (CSO Noxxon AG, Berlin): The evolution of a PhD thesis into a Biotech company - or how to get from bench to bedside

Wednesday 12 October

A1: Introductory course Particle and Astroparticle Physics: tba

A2: Introductory course Infection and Structural Biology, Prof. Dr. Henning Tidow (Institut für Biochemie und Molekularbiologie, Hamburg): Proteins - Structure and Function

'Proteins - Structure and Function'
Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, transport and store other molecules such as oxygen, provide mechanical support and immune protection, generate movement, transmit nerve impulses, and control growth and differentiation.

As the function of proteins is determined by their structure, structural biology is the key to understand the structure-function relationship of proteins. In my lecture, I will briefly introduce basic principles that determine the structure of proteins as well as experimental techniques that can be used to study protein structure. Selected examples will be used to illustrate the role of protein dynamics, conformational changes and protein-protein interactions in various physiological processes.

In the second part of the lecture series I will focus on membrane proteins and explain their special characteristics. Structure and function of different classes of integral membrane proteins will be introduced and discussed in relation to the biochemical/physiological processes they are involved in.

10:30 Coffee break

B1: Introductory course Photon Science, tba

B2: Introductory course Nanosciences, Karel Vyborny (Institute of Physics of the Czech Academy of Sciences, Prag): Introduction to selected phenomena of quantum transport

Introduction to selected phenomena of quantum transport
Electric conductivity - a prime example of a transport phenomenon - can be described classically in many cases. Electrons are thought of as point-like particles with definite velocity, accelerated by electric field which carry electric current. Quantum-mechanical view where electrons are considered waves is often leading to practically the same conclusions as the classical one. This course deals with a subjectively selected group of phenomena where the two pictures differ and genuine consequences of quantum mechanics become apparent. For example, the measured transversal resistivity in the Quantum Hall Effect exhibits steps quantized in the units of h/e^2 whereas it is strictly linear (without steps) in the applied magnetic field in its classical version. Given that the quantum mechanics describes microscopical objects (such as individual atoms), it is no surprise that many of these phenomena occur in devices with nanometre size and/or reduced dimensionality.
Syllabus: (1) Classical vs quantum transport. Basics of quantum mechanics. Heterostructures. (2) Conductance and thermopower quantisation in 1D. Tunneling through a quantum dot. (3) Aharonov-Bohm effect. Quantum Hall Effects. (4) Spintronics at nanoscale: magnetic tunneling junctions,
spin-orbit torques and ferromagnetic resonance.

12:30 Lunch break

C1: Focus course Photon Science: tba

C2: Focus course Infection and Structural Biology, Prof. Gerhard Wolber (FU Berlin): Structure based drug design II

In the second part of the structure-based drug design lectures, we will first focus on high-throughput virtual screening techniques using 3D pharmacophore interaction models. This technique allows for focusing on the most relevant binding features necessary for a small molecular ligand to bind to a protein. Together with the pre-calculation of potential ligand conformations, virtual screening can be performed at lower computational cost when compared to classical docking. In the absence of an experimentally determined crystal structure, 3D pharmacophores can even be used to extrapolate potential protein interaction points and used for virtual screening in a similar manner.1
We will then talk about purpose and limitations of molecular dynamics (MD) simulations2,3 in drug design: This technique can be used to sample different ligand conformations to partially sample protein flexibility up to a certain point. MD trajectories can be used to develop statistically enhanced interaction patterns (so-called ‘dynophores’) and help to better understand protein-ligand binding.
To illustrate the applicability of the presented algorithms, several success stories for predicting and understanding protein-ligand binding will be presented. These include the inhibition of sulfo- transferase 1E1 to avoid toxicity,4 development of novel molecules to modulate innate immunity through Toll-like receptors5,6 and explaining dual- and allosteric binding of ligands to the muscarinic acetylcholine receptor including their impact on biological function.7
References

1 Wolber, G., Seidel, T., Bendix, F. & Langer, T. Molecule-pharmacophore superpositioning and pattern matching in computational drug design. Drug Discov Today 13, 23-29, doi:Doi 10.1016/J.Drudis.2007.09.007 (2008).
2 Rakers, C., Bermudez, M., Keller, B. G., Mortier, J. & Wolber, G. Computational close up on protein–protein interactions: how to unravel the invisible using molecular dynamics simulations? WIREs Comput Mol Sci 5, 345- 359, doi:10.1002/wcms.1222 (2015).
3 Mortier, J., Rakers, C., Bermudez, M., Murgueitio, M. S., Riniker, S. & Wolber, G. The impact of molecular dynamics on drug design: applications for the characterization of ligand-macromolecule complexes. Drug Discov Today 20, 686-702, doi:10.1016/j.drudis.2015.01.003 (2015).
4 Rakers, C., Schumacher, F., Meinl, W., Glatt, H., Kleuser, B. & Wolber, G. In silico prediction of human sulfotransferase 1E1 activity guided by pharmacophores from molecular dynamics simulations. Journal of Biological Chemistry 291, 58-71, doi:10.1074/jbc.M115.685610 (2016).
5 Bock, S., Murgueitio, M. S., Wolber, G. & Weindl, G. Acute myeloid leukaemia-derived Langerhans-like cells enhance Th1 polarization upon TLR2 engagement. Pharmacological Research 105, 44-53, doi:10.1016/j.phrs.2016.01.016 (2016).
6 Murgueitio, M. S., Henneke, P., Glossmann, H., Santos-Sierra, S. & Wolber, G. Prospective Virtual Screening in a Sparse Data Scenario: Design of Small-Molecule TLR2 Antagonists. Chemmedchem 9, 813-822, doi:Doi 10.1002/Cmdc.201300445 (2014).
7 Schmitz, J., van der Mey, D., Bermudez, M., Klöckner, J., Schrage, R., Kostenis, E., Tränkle, C., Wolber, G., Mohr, K.
& Holzgrabe, U. Dualsteric Muscarinic Antagonists - Orthosteric Binding Pose Controls Allosteric Subtype Selectivity. J Med Chem 57, 6739-6750, doi:10.1021/jm500790x (2014).

C3: Soft skills I (group A)

C4: Soft skills II (group A)

15:30 Coffee break

D1: Focus course Particle and Astroparticle Physics: tba

D2: Focus course Nanoscience, Tobias Brandes (TU Berlin): Transport in nanostructures

This is a short introduction into some theoretical methods to describe transport through nanostructures. The focus is on relatively simple tools (such as master equations for quantum dots) which are useful in various situations with fluctuations and noise, Maxwell-demon and measurement-based feedback, and others.

D3: Soft skills I (group B)

D4: Soft skills II (group B)

17:30 Coffee Break

Poster session

Graduate Week BBQ

Thursday 13 October

A1: Introductory course Particle and Astroparticle Physics: tba

A2: Introductory course Infection and Structural Biology, Prof. Dr. Henning Tidow (Institut für Biochemie und Molekularbiologie, Hamburg): Proteins - Structure and Function

'Proteins - Structure and Function'
Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, transport and store other molecules such as oxygen, provide mechanical support and immune protection, generate movement, transmit nerve impulses, and control growth and differentiation.

As the function of proteins is determined by their structure, structural biology is the key to understand the structure-function relationship of proteins. In my lecture, I will briefly introduce basic principles that determine the structure of proteins as well as experimental techniques that can be used to study protein structure. Selected examples will be used to illustrate the role of protein dynamics, conformational changes and protein-protein interactions in various physiological processes.

In the second part of the lecture series I will focus on membrane proteins and explain their special characteristics. Structure and function of different classes of integral membrane proteins will be introduced and discussed in relation to the biochemical/physiological processes they are involved in.

10:30 Coffee break

B1: Introductory course Photon Science, tba

B2: Introductory course Nanosciences, Karel Vyborny (Institute of Physics of the Czech Academy of Sciences, Prag): Introduction to selected phenomena of quantum transport

Introduction to selected phenomena of quantum transport
Electric conductivity - a prime example of a transport phenomenon - can be described classically in many cases. Electrons are thought of as point-like particles with definite velocity, accelerated by electric field which carry electric current. Quantum-mechanical view where electrons are considered waves is often leading to practically the same conclusions as the classical one. This course deals with a subjectively selected group of phenomena where the two pictures differ and genuine consequences of quantum mechanics become apparent. For example, the measured transversal resistivity in the Quantum Hall Effect exhibits steps quantized in the units of h/e^2 whereas it is strictly linear (without steps) in the applied magnetic field in its classical version. Given that the quantum mechanics describes microscopical objects (such as individual atoms), it is no surprise that many of these phenomena occur in devices with nanometre size and/or reduced dimensionality.
Syllabus: (1) Classical vs quantum transport. Basics of quantum mechanics. Heterostructures. (2) Conductance and thermopower quantisation in 1D. Tunneling through a quantum dot. (3) Aharonov-Bohm effect. Quantum Hall Effects. (4) Spintronics at nanoscale: magnetic tunneling junctions,
spin-orbit torques and ferromagnetic resonance.

12:30 Lunch break

C1: Focus course Photon Science: tba

C2: Focus course Infection and Structural Biology, Prof. Gerhard Wolber (FU Berlin): Structure based drug design II

In the second part of the structure-based drug design lectures, we will first focus on high-throughput virtual screening techniques using 3D pharmacophore interaction models. This technique allows for focusing on the most relevant binding features necessary for a small molecular ligand to bind to a protein. Together with the pre-calculation of potential ligand conformations, virtual screening can be performed at lower computational cost when compared to classical docking. In the absence of an experimentally determined crystal structure, 3D pharmacophores can even be used to extrapolate potential protein interaction points and used for virtual screening in a similar manner.1
We will then talk about purpose and limitations of molecular dynamics (MD) simulations2,3 in drug design: This technique can be used to sample different ligand conformations to partially sample protein flexibility up to a certain point. MD trajectories can be used to develop statistically enhanced interaction patterns (so-called ‘dynophores’) and help to better understand protein-ligand binding.
To illustrate the applicability of the presented algorithms, several success stories for predicting and understanding protein-ligand binding will be presented. These include the inhibition of sulfo- transferase 1E1 to avoid toxicity,4 development of novel molecules to modulate innate immunity through Toll-like receptors5,6 and explaining dual- and allosteric binding of ligands to the muscarinic acetylcholine receptor including their impact on biological function.7
References

1 Wolber, G., Seidel, T., Bendix, F. & Langer, T. Molecule-pharmacophore superpositioning and pattern matching in computational drug design. Drug Discov Today 13, 23-29, doi:Doi 10.1016/J.Drudis.2007.09.007 (2008).
2 Rakers, C., Bermudez, M., Keller, B. G., Mortier, J. & Wolber, G. Computational close up on protein–protein interactions: how to unravel the invisible using molecular dynamics simulations? WIREs Comput Mol Sci 5, 345- 359, doi:10.1002/wcms.1222 (2015).
3 Mortier, J., Rakers, C., Bermudez, M., Murgueitio, M. S., Riniker, S. & Wolber, G. The impact of molecular dynamics on drug design: applications for the characterization of ligand-macromolecule complexes. Drug Discov Today 20, 686-702, doi:10.1016/j.drudis.2015.01.003 (2015).
4 Rakers, C., Schumacher, F., Meinl, W., Glatt, H., Kleuser, B. & Wolber, G. In silico prediction of human sulfotransferase 1E1 activity guided by pharmacophores from molecular dynamics simulations. Journal of Biological Chemistry 291, 58-71, doi:10.1074/jbc.M115.685610 (2016).
5 Bock, S., Murgueitio, M. S., Wolber, G. & Weindl, G. Acute myeloid leukaemia-derived Langerhans-like cells enhance Th1 polarization upon TLR2 engagement. Pharmacological Research 105, 44-53, doi:10.1016/j.phrs.2016.01.016 (2016).
6 Murgueitio, M. S., Henneke, P., Glossmann, H., Santos-Sierra, S. & Wolber, G. Prospective Virtual Screening in a Sparse Data Scenario: Design of Small-Molecule TLR2 Antagonists. Chemmedchem 9, 813-822, doi:Doi 10.1002/Cmdc.201300445 (2014).
7 Schmitz, J., van der Mey, D., Bermudez, M., Klöckner, J., Schrage, R., Kostenis, E., Tränkle, C., Wolber, G., Mohr, K.
& Holzgrabe, U. Dualsteric Muscarinic Antagonists - Orthosteric Binding Pose Controls Allosteric Subtype Selectivity. J Med Chem 57, 6739-6750, doi:10.1021/jm500790x (2014).

C3: Soft skills I (group A)

C4: Soft skills II (group A)

15:30 Coffee break

D1: Focus course Particle and Astroparticle Physics: tba

D2: Focus course Nanosciences: tba

D3: Soft skills I (group B)

D4: Soft skills II (group B)