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UID:20250928T083210EDT-23922UT4Nn@132.216.98.100
DTSTAMP:20250928T123210Z
DESCRIPTION:Electron transport (ETp)\, i.e.\, electronic conduction\, acros
 s peptides and proteins in a solid state–like configuration is remarkably 
 efficient\, comparable to that via completely conjugated molecules. From w
 ork with modified proteins\, and with homopeptides we find that both cofac
 tors and the secondary structure matter for the efficiency of the ETp.\n\n
 While ET and ETp are related\, nature regulates ET via redox chemistry\, w
 here control over the process is achieved at a price in free energy\, for 
 ETp no redox process is required. This allows studying ETp via non-redox p
 roteins\, such as the rhodopsins and albumins.\n	For most proteins (studied
  as monolayers) transport is thermally activated at > ~ 150 K\, but severa
 l proteins show temperature-independent transport from 15K till denaturati
 on\, including transport distances over 6 nm! The temperature-independent 
 current is the highest that such protein or its variants can carry\, as sh
 own for Azurin\, which exhibits clear Meyer-Neldel (compensation) behavior
 \, with the compensation temperature at denaturation.[1] As temperature-in
 dependence above the glass transition (~ 150K) is unlikely to be due to ba
 llistic transport\, tunneling is the probable mechanism. However\, the obs
 erved longer ETp distances are beyond those\, known even for completely co
 njugated organic molecules that allow efficient tunneling. This suggests a
  resonant process\, which raises the question of how a floppy system (prot
 ein\, peptide) can resonate at RT. This\, in turn fuels speculations on a 
 role for coherence in electron transport (as distinguished from energy tra
 nsfer)\, and (dis)proving this provides a challenge for experimentalists.
 \n\n1 N. Amdursky et al.\, Adv. Mater. 42\,7142-7161 (2014) Electronic Tra
 nsport via Proteins 10.1002/adma.201402304 (progress report)\;\n\nN. Amdur
 sky et al.\, Adv. Sci.\, 2015\, 2\, 1400026 Electron transfer proteins as 
 electronic conductors: Significance of the metal and its binding site in t
 he blue Cu protein\, Azurin\,  doi.org/10.1002/advs.201400026\n\n \n\n \n
 \n \n
DTSTART:20151020T170000Z
DTEND:20151020T183000Z
LOCATION:Room 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\
 , 801 rue Sherbrooke Ouest
SUMMARY:Chemical Society: Dr. David Cahen - Biomolecular Electronics: Elect
 ron Transport across Peptides and Proteins
URL:/chemistry/channels/event/chemical-society-dr-davi
 d-cahen-biomolecular-electronics-electron-transport-across-peptides-and-25
 6029
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