BEGIN:VCALENDAR VERSION:2.0 PRODID:www.dresden-science-calendar.de METHOD:PUBLISH CALSCALE:GREGORIAN X-MICROSOFT-CALSCALE:GREGORIAN X-WR-TIMEZONE:Europe/Berlin BEGIN:VTIMEZONE TZID:Europe/Berlin X-LIC-LOCATION:Europe/Berlin BEGIN:DAYLIGHT TZNAME:CEST TZOFFSETFROM:+0100 TZOFFSETTO:+0200 DTSTART:19810329T030000 RRULE:FREQ=YEARLY;INTERVAL=1;BYMONTH=3;BYDAY=-1SU END:DAYLIGHT BEGIN:STANDARD TZNAME:CET TZOFFSETFROM:+0200 TZOFFSETTO:+0100 DTSTART:19961027T030000 RRULE:FREQ=YEARLY;INTERVAL=1;BYMONTH=10;BYDAY=-1SU END:STANDARD END:VTIMEZONE BEGIN:VEVENT UID:DSC-17080 DTSTART;TZID=Europe/Berlin:20200227T130000 SEQUENCE:1582758444 TRANSP:OPAQUE DTEND;TZID=Europe/Berlin:20200227T140000 URL:https://www.dresden-science-calendar.de/calendar/en/detail/17080 LOCATION:TUD CRTD\, Fetscherstraße 10501307 Dresden SUMMARY:Troth-Petroczy: CMCB Life Sciences Seminar: Protein Sequence Space CLASS:PUBLIC DESCRIPTION:Speaker: Agnes Troth-Petroczy\nInstitute of Speaker: Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG) and Center for Systems Biology Dresden (CSBD)\nTopics:\nBiologie\n Location:\n Name: TU D CRTD (CRTD\, ground floor\, auditorium left)\n Street: Fetscherstraße 105\n City: 01307 Dresden\n Phone: +49 (0)351 458 82052\n Fax: +49 (0)3 51 458 82059 \nDescription:

Publications:

1.       Toth-P etroczy A*\, Palmedo P*\, John Ingraham JI\, Thomas A. Hopf TA\, Berger B\ , Sander C\, Marks DS. Structured states of disordered proteins f rom genomic sequences. Cell 2016\, 167(1):158-70.

2.        Rockah-Shmuel L\, Toth-Petroczy A\, Sela A\, Wurtzel O\, Sorek R and Tawfik DS. The Occurrence and Bypass of Frame-shifting Inse rtion-Deletions (InDels) to give Functional Proteins are correlated. PloS Genetics 2013 (10) e1003882

3.       Dellus-Gur E *\, Toth-Petroczy A*\, Elias M\, Tawfik DS. What makes a protein fold amenable to functional innovations? Fold polarity and stability trade -offs. J Mol Biol 2013\; 425(14):2609-21.

4.        Toth-Petroczy A and Tawfik DS. Protein insertions and deletion s enabled by neutral roaming in sequence space. Mol Biol Evol 2 013\; 30(4):761-71.

5.       Tóth-Petróczy A and Tawfik DS . Slow protein evolutionary rates are dictated by surface-core as sociation. PNAS 2011\, 108(27):11151-6.

Abstract:

Protein sequence space is vast\, the possibilities are astronomical\, y et only a tiny fraction of it is sampled by existing proteins. We mine evo lutionary information from millions of genomes to understand how protein f amilies evolve\, and what rules govern their functional and structural div ergence. We focus not only on genetic mutations but also on phenotypic mut ations\, i.e. mutations introduced by transcriptional and translational ma chinery. We wish to answer how proteins remain robust to mutations and fac ilitate innovations at the same time. We combine bioinformatics\, modellin g and experimental evolution to answer fundamental questions about molecul ar evolution.

Everybody is very welcome!

DTSTAMP:20260518T060748Z CREATED:20200206T230845Z LAST-MODIFIED:20200226T230724Z END:VEVENT END:VCALENDAR