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SUMMARY:Binding without folding: Extreme disorder and dynamics in a high-a
 ffinity protein complex  - Ben Schuler\, University of Zurich\, Department
  of Biochemistry and Department of Physics\, Zurich\, Switzerland
DTSTART:20180620T093000Z
DTEND:20180620T103000Z
UID:TALK106546@talks.cam.ac.uk
CONTACT:Patrick Flagmeier
DESCRIPTION:Molecular communication in biology is mediated by protein inte
 ractions. According to the current paradigm\, the specificity and affinity
  required for these interactions are encoded in the precise complementarit
 y of binding interfaces. Even proteins that are disordered under physiolog
 ical conditions or that contain large unstructured regions commonly intera
 ct with well-structured binding sites on other biomolecules. We recently d
 iscovered an unexpected interaction mechanism: The two intrinsically disor
 dered human proteins histone H1 and its nuclear chaperone prothymosin α a
 ssociate in a one-to-one complex with picomolar affinity\, but they fully 
 retain their structural disorder\, long-range flexibility\, and highly dyn
 amic character. Based on the close integration of single-molecule experime
 nts\, NMR\, and molecular simulations\, we obtained a detailed picture of 
 this complex that can be explained by the large opposite net charge of the
  two proteins without requiring defined binding sites or interactions betw
 een specific individual residues. This type of interaction has interesting
  ramifications for kinetic mechanisms of binding and cellular regulation.\
 n\nBorgia\, A.\, Borgia\, M.\, Bugge\, K.\, Kissling\, V.M.\, Heidarsson\,
  P.O.\, Fernandes\, C.B.\, Sottini\, A.\, Soranno\, A.\, Buholzer\, K.\, N
 ettels\, D.\, Kragelund\, B.B.\, Best\, R.B.\, & Schuler\, B. (2018) Extre
 me disorder in an ultra-high-affinity protein complex. Nature\, 555\, 61-6
 6.\n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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