Course summary

FEBS Advanced Course: Ligand-binding Theory and Practice

July 3 – July 10, 2016

Application deadline: April 1, 2016
Click on online application 

Registration fee 405 EUR

(Includes meals and accommodation, course materials, lab consumables, and social program)

Course Organizers: Jannette Carey, Rudiger Ettrich, Wei-Feng Xue

Location of the course:
Academy and University Center Nove Hrady, Czech Republic

This course provides training in the theoretical and practical principles of ligand binding. It offers participants the possibility to analyse their own macromolecular interaction systems using contemporary advanced methods including surface plasmon resonance, isothermal titration calorimetry, UV-vis and fluorescence spectroscopies, and microscale thermophoresis. The design, execution, and interpretation of these experiments will be guided by expert tutors. Additional lecturers will discuss other contemporary methods used in experimental studies of ligand binding, and current views on the phenomenon of allostery.

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Detailed description

Intermolecular interactions – between or among proteins, nucleic acids, or small molecules – underlie virtually every aspect of biology. Quantitative analysis of these interactions to determine their affinity, specificity, stoichiometry, cooperativity (allostery), and kinetics is a required first step toward understanding their biological roles. Recent developments in a range of new analytical methods have made direct quantitative study of macromolecular interactions readily accessible even to those with limited background in ligand-binding theory. Although the theory is rooted in the most elementary principles of general chemistry, it is very often applied poorly, leading to incorrect or ambiguous results, many of which have found their way into the literature over the years, limiting our understanding of interactions in important biomolecular systems.

This course will provide basic training in the principles of ligand-binding theory, and will offer students a chance to analyse their own macromolecular interaction systems using the contemporary advanced methods of surface plasmon resonance SPR, isothermal titration calorimetry ITC, UV-vis and fluorescence spectroscopies, and microscale thermophoresis, guided by lecturers and tutors who are experts in the design, execution, and analysis of these experiments. Students will also gain exposure to contemporary experimental ligand-binding methods that are not represented among the practicals, including NMR, mass spectrometry, analytical ultracentrifugation AUC, vibrational spectroscopies, and others, through presentations by lecturers who are expert in each method. Besides ligand binding per se, a second unifying theme of the lectures will be allostery, also known as cooperativity. Nobelist Jacques Monod is said to have regarded allostery as life’s second secret, and study of allosteric mechanisms is widely regarded as the most important contemporary application of ligand-binding studies. Among the lecturers on allostery will be experts who will debate our current understanding of hemoglobin, the most well-known biological manifestation of cooperative ligand binding.

The course is aimed for practitioners of ligand binding at the graduate or early postdoctoral level, although our experience indicates that even more advanced practitioners will also increase their competency, enabling them to disseminate an accurate understanding of this critical topic. Basic training in the fundaments of ligand-binding theory will open the course, to enable all students to acquire the principles that can support their experiments and leverage the subsequent lecture program of expert speakers. This training will also equip students with the skills to critically evaluate published binding data in any molecular system. The first half-day will include lectures, group discussion, and problem-solving exercises in a first seminar directed by Prof. Jannette Carey, and computational analysis, simulation, and data analysis in a workshop directed by Prof. Wei-Feng Xue. The course will conclude with a workshop on global analysis of each student’s own ligand binding results in a seminar directed by Prof. Xue.

All accepted students will be advised to bring experimental samples that can be suited for the available laboratory practicals. The organizers will work closely in advance with the selected applicants to prioritize for each student the practicals that are most likely to yield usable data for each student’s system, and to ensure they bring with them materials that are appropriate for each practical.
Students are expected to bring posters that introduce their research project, illustrate the role of ligand binding studies in their project, and explain why the methods of this course are expected to be useful for their work. The organizing committee assisted by selected speakers will evaluate the posters, and choose approximately one-third of the students to present their work to the entire group of participants (students, speakers, tutors, organizers, and guests). Poster speakers will be announced at the welcome introduction on Monday morning, and will be scheduled for fifteen-minute talks during three successive morning lecture sessions later in the week. Posters will remain available all week in the social hall to stimulate discussion among all participants.

All students will present the results of their experiments in this course in a final morning session, with 10-minute talks each.

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