Course: Protein structures

Protein structures: production, prowess, power, promises, and problems

Date

4 November 2015 – 8 November 2015, CMBI, NCMLS, Nijmegen, the Netherlands

Lecturers

  • Gert Vriend, CMBI, course coördinator, g.vriend@cmbi.ru.nl
  • Daniel Hoffmann , University Duisburg/Essen (TBC)
  • Robbie Joosten, Netherlands Cancer Institute
  • Hanka Venselaar, CMBI
  • Wouter Touw, CMBI

Location

Center for Molecular and Biomolecular Informatics (CMBI), Radboud University Nijmegen-Medical Centre /NCMLS, Nijmegen, the Netherlands

Target audience

The course is suitable for both PhD students working in structural bioinformatics as well as for PhD students in the life sciences who want to learn more about using structural informatioin in their research. The course schedule accommodates both groups, parallel sessions for both groups will be scheduled when necessary.

Study load

3 EC

Course description

In the right hands, protein structures are a ‘power’ful tool to answer bio-molecular questions. Knowledge of the structure is a pre-requisite for rational drug design, for biotechnology, for chemical biology, and for answering a whole series of biomedical questions. In this course we will discuss the ‘production’ of protein structures by NMR, X-ray, and homology modelling. These methods all have their pro’s and cons so a certain ‘prowess’ is needed to follow all ‘promises’ and start attacking bio-medical ‘problems’ using protein structures.

The course will be split in three parts.

  • Part 1) Looking and seeing things in protein structures, learning to operate the software, understanding some of the algorithms.
  • Part 2) Protein structure determination (prediction) with NMR, X-ray, and homology modelling, and the possibilities and problems that come with each of these three techniques.
  • Part 3) Applying all that was learned in real-life example studies.

Examples of questions you will be able to answer after follwing the course:

  • Why is a person with this mutation sick? Or in other words, how does the molecular phenotype cause a disease state?
  • This enzyme converts mannose. Can I make is specificity broader?
  • This enzyme doesn’t function in my in vitro assay. Should I add some ions?
  • I want to add a tag to my enzyme, should I put it on the N-terminus, the C-terminus, or is something different needed?
  • This receptor binds a ligand, but if I look at the structure, that ligand doesn’t fit at all. Can I predict motions that take place upon ligand binding?

Concept course schedule

Day 1: Homology modelling seminar (H Venselaar).

YASARA practicals

  • Watching and seeing protein structures
  • Homology modelling
  • Answering biological/biomedical questions using protein structures and models”.

Day 2: Protein structure determination and validation seminars (R Joosten, G Vriend).

Practicals

  • X-ray and NMR structure comparison
  • Protein structure validation and implications

Day 3: Electrostatics and molecular dynamics seminars (D Hoffmann).

Practicals

  • Role of electrostatics
  • Answering biological questions with MD

Day 4: Protein structure comparison seminars (Guest, H Venselaar, G Vriend).

Practicals

  • Sequences analysis when structure data is available
  • Answering medical questions with sequence-structure alignments

Day 5: Own project executed with help from CMBI staff.

Registration and course fee

You can register for this course and find information about the fee on the enrolment page[LINK]. The maximum number of participants is 20 so register soon to be sure of a course seat!

The fee includes:

  • Course material: Handouts will be handed out at the start of the course. Software required for the lab course will be made available online.
  • Catering: Coffee, tea and soft drinks and lunch will be provided.

For more information about the course programme you can contact Celia van Gelder.

You can pre-register for the course via the pre-registration form.

Previous courses

2013 Edition

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