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SUMMARY:Non-Equilibrium Coupling of Protein Structure and Function to Tran
 slation Elongation Kinetics
DTSTART:20181019T140000
DTSTAMP:20260919T231426Z
UID:86f430404ff0ffc9051a5c73999a4e7a70f2faa2d2c52850f15c1239
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Edward O'brien\, Department of Chemistry\, Pennsylvania
  State University\, University Park\, PA (USA)\nSEMINAR IN BIOLOGICAL AND 
 STATISTICAL PHYSICS\n\nAbstract:\nProtein folding research has been domina
 ted by the assumption that thermodynamics determines protein structure and
  function. And that when the folding process is compromised\, the proteost
 asis machinery of cells - chaperones\, deaggregases\, the proteasome - wor
 k to restore proteins to their soluble\, functional form or degrade them t
 o maintain the cellular pool of proteins in a quasi-equilibrium state. Dur
 ing the past decade\, however\, more and more proteins have been identifie
 d for which altering only their speed of synthesis alters their structure 
 and function\, the efficiency of the down-stream processes they take part 
 in\, and cellular phenotype. Indeed\, evidence has emerged that evolutiona
 ry selection pressures have encoded translation-rate information into mRNA
  molecules to coordinate diverse co-translational processes. Thus\, non-eq
 uilibrium physics can play a fundamental role in influencing nascent prote
 in behavior\, mRNA sequence evolution\, and disease. I will discuss my lab
 s efforts to understand this non-equilibrium coupling through the developm
 ent and application of theoretical and computational methods\, including c
 oarse-grained simulations\, chemical kinetics\, statistical mechanics\, an
 d physical bioinformatics.\n\nBio: Assistant Professor of Chemistry\nPost-
 doc\, University of Cambridge\, 2013\nPh.D. Chemical Physics\, University 
 of Maryland College Park\, 2008\nB.S. Biochemistry\, University of the Sci
 ences\, 2002
LOCATION:BSP 727 https://plan.epfl.ch/?room==BSP%20727
STATUS:CONFIRMED
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