Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.3 extracted from

  • Kozlowski, R.; Zhao, J.; Dyer, R.B.
    Acceleration of catalysis in dihydrofolate reductase by transient, site-specific photothermal excitation (2021), Proc. Natl. Acad. Sci. USA, 118, e2014592118 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis study of protein dynamics, using a pump-probe method that employs pulsed-laser photothermal heating of a gold nanoparticle (AuNP) to directly excite a local region of the protein structure and transient absorbance to probe the effect on enzyme activity. Activity is accelerated by pulsed-laser excitation when the AuNP is attached close to a network of coupled motions in DHFR. No rate acceleration is observed when the AuNP is attached away from the network with pulsed excitation, or for any attachment site with continuous wave excitation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
-
-

General Information

General Information Comment Organism
metabolism study of protein dynamics, using a pump-probe method that employs pulsed-laser photothermal heating of a gold nanoparticle (AuNP) to directly excite a local region of the protein structure and transient absorbance to probe the effect on enzyme activity. Activity is accelerated by pulsed-laser excitation when the AuNP is attached close to a network of coupled motions in DHFR. No rate acceleration is observed when the AuNP is attached away from the network with pulsed excitation, or for any attachment site with continuous wave excitation Escherichia coli