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SUMMARY:Visualizing rare conformational states of proteins by solution NMR
  - Dr Guillaume Bouvignies\, ENS Paris
DTSTART:20170124T103000Z
DTEND:20170124T113000Z
UID:TALK70726@talks.cam.ac.uk
CONTACT:23027
DESCRIPTION:Much of structural biology to date has focused on the determin
 ation of three-dimensional models of biomolecules and the subsequent inter
 pretation of these models to explain or better understand biological funct
 ion. This is a critical first step and in many cases the pictures produced
  have generated invaluable insight. Yet\, biological molecules such as pro
 teins are often dynamic\, with their function being modulated by exchange 
 between different conformations. Therefore\, a complete understanding of t
 he relation between a biomolecule's structure\, dynamics and function requ
 ires the description of both the native-state conformations and all the ot
 her conformers that exchange with it. The task is\, however\, challenging 
 because many of these conformers are only transiently formed and marginall
 y populated\, so that they cannot be individually characterized by most bi
 ophysical tools. Modern NMR spectroscopy provides some of the most powerfu
 l techniques for detecting and characterizing such minor states. In this t
 alk\, some of these NMR methods will be described\, along with an applicat
 ion to the study of a cavity mutant of T4 lysozyme that binds small hydrop
 hobic molecules and transiently populates a higher-energy state. In additi
 on\, I will show how the same methodology can be applied to characterize t
 he highly dynamic complex of the intrinsically disordered C-terminal domai
 n of the protein Artemis\, which folds upon binding to the DNA binding dom
 ain of Ligase IV. Structural model of the complex can be obtained with no 
 direct observation of the signals of the bound form of Artemis.
LOCATION:Unilever Lecture Theatre\,  Department of Chemistry
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