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SUMMARY:De novo Design of Transmembrane Helix-Helix Interactions in Membra
 ne Proteins - Dr Anne Dixon\, University of Warwick
DTSTART:20160524T150000Z
DTEND:20160524T160000Z
UID:TALK63380@talks.cam.ac.uk
CONTACT:Alice Wood
DESCRIPTION:Membrane proteins regulate a large number of cellular function
 s\, and have great potential as tools for manipulation of biological syste
 ms. Developing these tools requires a robust and quantitative understandin
 g of membrane protein folding and interactions within the bilayer.  Over t
 he last 10 years\, we have used a wide range of biophysical and biochemica
 l tools to better understand the rules of engagement for native protein se
 quences in membranes and membrane mimetics.  From these studies\, and simi
 lar studies in labs across the world\, a link between transmembrane domain
  sequence “motifs” and protein-protein interaction propensity has emer
 ged.  We have utilized this information to design a series of proteins to 
 probe the net thermodynamic contribution of well-known sequence motifs to 
 transmembrane helix-helix association in a biological membrane.  We have q
 uantified the apparent free energy contribution of a range of motifs to tr
 ansmembrane helix self-association in a biological membrane\, and our init
 ial results suggest that the free energy barrier to overcoming weak associ
 ation is quite small.  This work has allowed us to rationalize the contrib
 ution of key motifs to transmembrane helix association\, and offers a rout
 e to direct the design of novel sequences for use in biotechnology or synt
 hetic biology.  
LOCATION:Unilever Lecture Theatre\, Department of Chemistry
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