15–17 May 2017
Oxford Spires Hotel
Europe/Stockholm timezone

Studying bacterial membrane protein complexes by the use of contrasting components

Not scheduled
20m
Oxford Spires Hotel

Oxford Spires Hotel

Abingdon Rd Oxford OX1 4PS UK
Invited Speaker Protein structure and function

Description

Gram-negative bacteria include agents responsible for meningitis, plague, Legionnaire’s Disease, gonorrhoea, urinary tract infections, pneumonia, cholera and sepsis. They possess a characteristic outer membrane (OM) which, by acting as a molecular sieve, controls access to the more fragile inner membrane. This OM is an unusual asymmetric bilayer with an external monolayer of lipopolysaccharide (LPS) and an inner layer of phospholipids. This means that the OM is robust and highly impermeable to toxins or antibiotics. Access to the periplasm, between the membranes, is controlled by integral outer membrane proteins (OMP) which filter molecules by size or by selective uptake of desirable larger molecules such as vitamins and sugars. This unique structure is the first line in the resistance of bacteria to antibiotics and our goal is to understand its structure and stability. My lecture will show how neutrons, with their ability to distinguish different molecular contrasts, can provide information unavailable from other techniques. The deuteration of one OMP has enabled us to exploit a range of other contrasts to unveil protein-protein, protein-lipid and protein-surfactant interactions.

Primary author

Prof. Jeremy Lakey (Newcastle University)

Presentation materials

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