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UID:20250821T211039EDT-3550UHWtrz@132.216.98.100
DTSTAMP:20250822T011039Z
DESCRIPTION:In photosynthetic light harvesting\, absorbed energy migrates t
 hrough a protein network to reach a dedicated location for conversion to c
 hemical energy. This energy flow is efficient\, directional\, and\, in oxy
 genic photosynthesis\, regulated. The regulatory response\, known as non-p
 hotochemical quenching (NPQ)\, involves complex and complicated multi-time
 scale processes that safely dissipate excess energy\, thus protecting the 
 system against deleterious photoproducts. In recent research\, a protein w
 ithin this network\, light-harvesting complex stress related (LHCSR)\, has
  been implicated in regulation in green algae and moss. However\, the mech
 anisms behind photoprotection that occur in LHCSR remain poorly understood
 . We explore these mechanisms by probing LHCSR at the single-protein level
 \, enabling us to separate and identify distinct conformations. By charact
 erizing the conformational states and dynamics of individual proteins\, we
  characterize energy dissipation in single LHCSR proteins and how the exte
 nt of dissipation changes in response to pH and carotenoid composition\, t
 wo components known to play a role in photoprotection. From this informati
 on\, we identify the role of individual complexes in the balance between e
 fficiency and adaptability in photosynthetic light harvesting.\n
DTSTART:20161004T170000Z
DTEND:20161004T183000Z
LOCATION:Rm 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\, 
 801 rue Sherbrooke Ouest
SUMMARY:Chemical Society Seminar: Dr. Gabriela Schlau-Cohen - Single-molecu
 le exploration of the regulation of photosynthetic light harvesting 
URL:/chemistry/channels/event/chemical-society-seminar
 -dr-gabriela-schlau-cohen-single-molecule-exploration-regulation-261952
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