Biophysical techniques for studying components of biological membranes

Posted on: 30/01/2019

The Biochemical Society is running a training workshop on membrane proteins on 3-5 April in Leeds.

The ‚ÄòCrossing Biological Membranes‚Äô Network (CBMNet) is¬†sponsoring a Biochemical Society Training Event¬†on Membrane Proteins: Solubilisation and Biophysical Characterisation, which will take place on 3rd – 5th April 2019 at the University of Leeds.

This three-day training event for early career researchers will focus on the function of biological membranes and on the biophysical techniques available to study their components in the context of biology and biotechnology. The event will comprise lectures, computer and laboratory-based practical sessions. Participants will leave the event with new knowledge and protocols that will allow them to use biophysical techniques for studying components of biological membranes in their research.

Topics include:

  • Solubilisation and purification of lipid nanoparticles (SMALPs)
  • Structural elucidations, cryo-EM & crystallography
  • Spectroscopy of membranes and membrane proteins, circular dichroism & EPR
  • Modelling membranes and membrane proteins
  • Validation of membrane protein structures
  • Lipidomics and membrane protein mass spectroscopy
  • Single-molecular and single-enzyme studies of membrane proteins

Early bird registration closes Friday 8 March 2019. You can find out more and register here.

CBMNet is a BBSRC Network in Industrial Biotechnology and Bioenergy (BBSRC NIBB), designed to foster collaborations between academia, industry, policy makers and NGOs in order to find new approaches to tackle research challenges, translate research and deliver key benefits in Industrial Biotechnology and Bioenergy (IBBE).

CBMNet has worked towards advancing understanding of the the mechanisms by which substances are transported into, within and out of cell factories, which will lead to the development of enabling technologies that are crucial for the future development of almost all cell-based IBBE applications.

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