BEGIN:VCALENDAR

VERSION:2.0

PRODID:-//wp-events-plugin.com//7.2.2.1//EN

TZID:Asia/Jerusalem

X-WR-TIMEZONE:Asia/Jerusalem
BEGIN:VEVENT

UID:1185@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20230711T130000

DTEND;TZID=Asia/Jerusalem:20230711T133000

DTSTAMP:20230703T081623Z

URL:https://biology.technion.ac.il/en/seminars/msc-graduate-seminar-nitsan
 -yehi-shalom/

SUMMARY:MSc. Graduate Seminar-Nitsan Yehi Shalom [No Categories]
DESCRIPTION:Location: hybrid- in the Faculty Auditorium/ZOOM:https://techni
 on.zoom.us/j/97047969393   \n Affiliation: \n Host:Prof. Schuster Gadi \, 
 Prof. Bronstein Alexander and Dr. Marx Ailie  \n Silently Shaping Structur
 e- Exploring the role of synonymous genetic coding in shaping the local pr
 otein backbone structure\n\nIn the mid-20th century Christian Anfinsen\, l
 ater Nobel Prize winner\, showed that RNaseA can be denatured to lose stru
 cture and function and then subsequently renatured to regain both\, settin
 g the bedrock of our understanding of what governs protein folding. His ex
 periments suggested that proteins carry no memory of the genetic sequence 
 from which they were translated\, despite 18 out of the 20 amino acids bei
 ng translated from non-unique\, synonymous\, codons. Subsequently\, geneti
 c alterations leaving the amino acid sequence unchanged were termed and la
 rgely considered `silent`. Later findings demonstrated that synonymous mut
 ations can alter translation speeds and accuracy affecting co-translationa
 l folding and the overall\, globular\, structure of the resultant protein.
  We have recently shown that synonymous codon usage is associated with the
  local structure (backbone dihedral angle distribution) of the translated 
 amino acid. However\, these computational results are unable to establish 
 causality\; the association may be evolutionary\, or an active translation
 -dependent effect. The goal of this project is to explore the latter\; can
  synonymous mutations alter the local structure of the encoded amino acids
 ? We are exploring this hypothesis by targeting proteins that on one hand 
 give high-resolution X-ray diffraction patterns and on the other hand cont
 ain short noninteracting sequences whose initial (codon- sensitive) struct
 ure should be minimally affected by protein folding. 
LOCATION:hybrid- in the Faculty Auditorium/ZOOM:https://technion.zoom.us/j/
 97047969393 

END:VEVENT

BEGIN:VTIMEZONE

TZID:Asia/Jerusalem

X-LIC-LOCATION:Asia/Jerusalem

BEGIN:DAYLIGHT

DTSTART:20230324T030000

TZOFFSETFROM:+0200

TZOFFSETTO:+0300

TZNAME:IDT

END:DAYLIGHT

END:VTIMEZONE
END:VCALENDAR