BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Biomedical Mathematics Group - ECPv6.15.20//NONSGML v1.0//EN
CALSCALE:GREGORIAN
METHOD:PUBLISH
X-ORIGINAL-URL:https://www.ibs.re.kr/bimag
X-WR-CALDESC:Events for Biomedical Mathematics Group
REFRESH-INTERVAL;VALUE=DURATION:PT1H
X-Robots-Tag:noindex
X-PUBLISHED-TTL:PT1H
BEGIN:VTIMEZONE
TZID:Asia/Seoul
BEGIN:STANDARD
TZOFFSETFROM:+0900
TZOFFSETTO:+0900
TZNAME:KST
DTSTART:20220101T000000
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTART;TZID=Asia/Seoul:20230609T140000
DTEND;TZID=Asia/Seoul:20230609T160000
DTSTAMP:20260425T200537
CREATED:20230529T032327Z
LAST-MODIFIED:20230608T050231Z
UID:7805-1686319200-1686326400@www.ibs.re.kr
SUMMARY:Seokjoo Chae\, The energy cost and optimal design of networks for biological discrimination
DESCRIPTION:We will discuss about “The energy cost and optimal design of networks for biological discrimination”\, Yu\, Qiwei\, Anatoly B. Kolomeisky\, and Oleg A. Igoshin.\, Journal of the Royal Society Interface 19.188 (2022): 20210883. \nAbstract \n\n\nMany biological processes discriminate between correct and incorrect substrates through the kinetic proofreading mechanism that enables lower error at the cost of higher energy dissipation. Elucidating physico-chemical constraints for global minimization of dissipation and error is important for understanding enzyme evolution. Here\, we identify theoretically a fundamental error–cost bound that tightly constrains the performance of proofreading networks under any parameter variations preserving the rate discrimination between substrates. The bound is kinetically controlled\, i.e. completely determined by the difference between the transition state energies on the underlying free energy landscape. The importance of the bound is analysed for three biological processes. DNA replication by T7 DNA polymerase is shown to be nearly optimized\, i.e. its kinetic parameters place it in the immediate proximity of the error–cost bound. The isoleucyl-tRNA synthetase (IleRS) of E. coli also operates close to the bound\, but further optimization is prevented by the need for reaction speed. In contrast\, E. coli ribosome operates in a high-dissipation regime\, potentially in order to speed up protein production. Together\, these findings establish a fundamental error–dissipation relation in biological proofreading networks and provide a theoretical framework for studying error–dissipation trade-off in other systems with biological discrimination.
URL:https://www.ibs.re.kr/bimag/event/2023-06-09-jc/
LOCATION:B378 Seminar room\, IBS\, 55 Expo-ro Yuseong-gu\, Daejeon\, 34126\, Korea\, Republic of
CATEGORIES:Journal Club
ORGANIZER;CN="Jae Kyoung Kim":MAILTO:jaekkim@kaist.ac.kr
END:VEVENT
END:VCALENDAR