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SUMMARY:EPFL BioE Talks SERIES  "Revealing Evolutionary Constraints on Pro
 teins Through Sequence Analysis"
DTSTART:20201123T163000
DTEND:20201123T170000
DTSTAMP:20260415T032247Z
UID:060c9a51e31f2030fc1ec239fd61aaab7b9ff08a8ddd63dc95e41b27
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Anne-Florence Bitbol\, Institute of Bioengineering\, EPF
 L\, Lausanne (CH)\nWEEKLY EPFL BIOE TALKS SERIES\n\n(note that this talk i
 s number two of a double-feature seminar - see details of the first talk h
 ere)\n\nAbstract:\nProteins play crucial parts in all cellular processes\,
  and their functions are encoded in their amino-acid sequences. Statistica
 l analysis of alignments of large numbers of protein sequences has reveale
 d “sectors” of collectively coevolving amino acids in several protein 
 families. What is the origin of these sectors? We show that selection acti
 ng on any functional property of a protein\, represented by an additive tr
 ait\, can give rise to such a sector. As an illustration of a selected tra
 it\, we consider the elastic energy of an important conformational change 
 within an elastic network model\, and we show that selection acting on thi
 s energy leads to correlations among residues. For this concrete example a
 nd more generally\, we demonstrate that the main signature of functional s
 ectors lies in the small-eigenvalue modes of the covariance matrix of the 
 selected sequences. However\, secondary signatures of these functional sec
 tors also exist in the extensively-studied large-eigenvalue modes. Our sim
 ple\, general model leads us to propose a principled method to identify fu
 nctional sectors\, along with the magnitudes of mutational effects\, from 
 sequence data. We further demonstrate the robustness of these functional s
 ectors to various forms of selection\, and the robustness of our approach 
 to the identification of multiple selected traits. A better understanding 
 of protein sectors will make it possible to discern collective protein pro
 perties directly from sequences\, as well as to design new functional sequ
 ences.\n\n\nBio:\nAnne-Florence Bitbol studied physics at ENS Lyon.  Her 
 PhD at Université Paris-Diderot\, advised by Prof. Jean-Baptiste Fournier
 \, focused on the statistics and dynamics of complex membranes\, using sta
 tistical and soft matter physics to understand how lipid bilayers are pert
 urbed by proteins or by local chemical perturbations. She then chose to mo
 ve even closer to biology\, as a postdoc in the Biophysics Theory Group at
  Princeton University\, led by Profs. Ned Wingreen\, Bill Bialek and Curt 
 Callan. There\, she investigated the self-assembly of multi-protein comple
 xes\, and she also worked on evolution in rugged fitness landscapes with D
 avid Schwab. Next\, she became a CNRS researcher at Laboratoire Jean Perri
 n\, Institut de Biologie Paris-Seine\, Sorbonne Université in Paris\, and
  she recently moved to EPFL\, where she is a Tenure-Track Assistant Profes
 sor in the Institute of Bioengineering and the School of Life Sciences. Sh
 e is broadly interested in understanding biological phenomena in a quantit
 ative way\, through physical concepts as well as mathematical and computat
 ional tools. Her current research focuses on two main axes: the sequence-f
 unction mapping in proteins\, and the evolution of microbes on complex fit
 ness landscapes\, with application to antimicrobial resistance evolution.\
 n\n\n\nZoom link (with registration) for attending remotely: https://go.ep
 fl.ch/EPFLBioETalks\n\n\nIMPORTANT NOTICE: due to restrictions resulting f
 rom the ongoing Covid-19 situation\, this seminar can be followed via Zoom
  web-streaming only\, following prior one-time registration through the li
 nk above.
LOCATION:via Zoom web-streaming only\, due to Covid-19 situation https://g
 o.epfl.ch/EPFLBioETalks https://go.epfl.ch/EPFLBioETalks
STATUS:CONFIRMED
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