BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//UCLA - ECPv5.14.1//NONSGML v1.0//EN
CALSCALE:GREGORIAN
METHOD:PUBLISH
X-WR-CALNAME:UCLA
X-ORIGINAL-URL:https://www.chemistry.ucla.edu
X-WR-CALDESC:Events for UCLA
REFRESH-INTERVAL;VALUE=DURATION:PT1H
X-Robots-Tag:noindex
X-PUBLISHED-TTL:PT1H
BEGIN:VTIMEZONE
TZID:America/Los_Angeles
BEGIN:DAYLIGHT
TZOFFSETFROM:-0800
TZOFFSETTO:-0700
TZNAME:PDT
DTSTART:20230312T100000
END:DAYLIGHT
BEGIN:STANDARD
TZOFFSETFROM:-0700
TZOFFSETTO:-0800
TZNAME:PST
DTSTART:20231105T090000
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20231016T160000
DTEND;TZID=America/Los_Angeles:20231016T170000
DTSTAMP:20260614T090946
CREATED:20230816T014829Z
LAST-MODIFIED:20231012T212307Z
UID:30827-1697472000-1697475600@www.chemistry.ucla.edu
SUMMARY:Physical Chemistry Seminar 228: Rodrigo Noriega
DESCRIPTION:Noriega Flyer \nTitle: Study and Regulation of Biomolecular Interactions at Electrified Interfaces \nAbstract: We seek to understand the role of electrostatic interactions in molecular recognition mechanisms that are sensitive to structure but not sequence. An interesting model system for these multifaceted interactions is Loquacious-PD (Loqs-PD)\, a co-factor protein with two RNA binding motifs that recognize double-stranded RNA (dsRNA) regardless of their terminus structure. Loqs-PD regulates the terminus-dependent binding of the endonuclease enzyme Dicer-2 and is crucial to the efficient processing of sub-optimal dsRNA targets with a 3’ overhang terminus for gene silencing in Drosophila melanogaster. \nTo identify the effects of electrostatics and local dynamics on the formation and stability of dsRNA:Loqs-PD complexes\, we study their binding and dynamics at electrified interfaces with a combination of mid-infrared surface plasmonics\, time-resolved ultrafast fluorescence\, and in situ electrochemical experiments at the surface of a degenerately doped wide-gap metal oxide. In this way\, we distinguish distinct stages in the binding event between an RNA-binding protein and its target and follow dynamic events over multiple time scales. Time-resolved fluorescence measurements show a high affinity interaction that is strongly affected by electric fields\, while mid-infrared surface plasmon observations detect a lower affinity interaction with a reduced (but still substantial) sensitivity to electric fields. In both cases\, fluctuations are dependent on protein binding and the presence of electric fields. \nMulti-stage binding process that arise from non-specific interactions are common between nucleic acids and proteins\, and studies that employ complementary observations under controlled perturbations are a powerful tool to interrogate the link between molecular recognition and biochemical function. \n 
URL:https://www.chemistry.ucla.edu/events/physical-chemistry-seminar-228-rodrigo-noriega/
LOCATION:Mani L. Bhaumik Centennial Collaboratory\, 607 Charles E. Young Dr.\, East\, Los Angeles\, CA\, 90095\, United States
CATEGORIES:Physical Chemistry Seminar
END:VEVENT
END:VCALENDAR