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SUMMARY:Probing Protein–DNA Recognition\, Binding\, and Function with No
 nlinear Spectroscopy and Single-Molecule Optical Techniques
DTSTART:20260706T090000Z
DTEND:20260706T110000Z
DTSTAMP:20260703T223000Z
UID:indico-event-1871@indico.dfa.unipd.it
CONTACT:silvana.schiavo@unipd.it
DESCRIPTION:Speakers: Andy Marcus (University of Oregon)\n\n\nLunedi 6 lug
 lio 2026 - Ore 11 Aula Voci\n\n \nProf. Andy Marcus\nUniversity of Oregon
 \n \n \n\nTitle: \nProbing Protein–DNA Recognition\, Binding\, and Fu
 nction with Nonlinear Spectroscopy and Single-Molecule Optical Techniques
  \n \nAbstract: \nProteins that interact with DNA must locate specific 
 target sites within the genome\, recognize appropriate structural and sequ
 ence features\, and carry out tightly regulated functional processes such 
 as replication\, transcription\, and repair. Despite extensive study\, the
  molecular mechanisms that couple DNA recognition and binding to biologica
 l function remain incompletely understood\, particularly on the time and l
 ength scales relevant to dynamic cellular environments.\nIn this work\, we
  employ a combination of nonlinear spectroscopic methods and single-molecu
 le optical techniques to investigate the mechanisms of protein–DNA recog
 nition\, binding\, and function. Multidimensional fluorescence-detected sp
 ectroscopy provides access to coherent and incoherent dynamical processes\
 , enabling us to resolve heterogeneous structural ensembles and characteri
 ze couplings between electronic states in labeled nucleic acid systems. Co
 mplementary single-molecule approaches allow direct observation of stochas
 tic binding events\, conformational transitions\, and functional activity 
 in real time\, revealing distributions of pathways and intermediates that 
 are obscured in ensemble measurements.\nBy integrating these approaches\, 
 we map the free-energy landscapes that govern protein–DNA interactions\,
  linking structural fluctuations and binding specificity to functional out
 comes. We illustrate these principles through studies of specific systems\
 , including the T4 bacteriophage single-stranded DNA binding protein (gp32
 )\, the T4 clamp–clamp loader complex\, and the E. coli lactose repress
 or–operator system. These examples provide new insights into how protein
 s recognize their DNA targets and how this recognition couples to biologic
 al function\, offering a more complete physical picture of the molecular m
 achines that underlie genome expression.\n\n \n \n \n\nhttps://indico.d
 fa.unipd.it/event/1871/
LOCATION:1/1-2 - Aula "C. Voci" (Dipartimento di Fisica e Astronomia - Edi
 ficio Marzolo)
URL:https://indico.dfa.unipd.it/event/1871/
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