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SUMMARY:Towards More Physical Models of Enzyme Active Sites Using Quantum M
 echanics
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20231116T160000
UID:2026-05-19-17-14-43@natsci.colostate.edu
DTSTAMP:20260519T171443
Description:Abstract:\n\nEnzymes are highly efficient catalysts and essenti
 al to life\, prompting significant research into how they function. Unders
 tanding various structural or electronic properties of enzymes and how the
 y contribute to enzymatic function will help researchers take advantage of
  catalytic motifs and design bioinspired molecular catalysts. There are se
 veral methods of computationally studying enzymatic reactions which focus 
 on different interactions\, ranging from Molecular Dynamics simulations to
  Quantum Mechanical (QM) cluster models of enzymes. In the QM cluster appr
 oach\, the active site of the enzyme is extracted from the surrounding pro
 tein and constraints are put on anchor atoms\, where residues are no longe
 r bound by surrounding protein\, during geometry optimization to mimic str
 uctural constraints. Most QM cluster models fix the crystallographic posit
 ions of anchor atoms\, sometimes leading to unphysical results and ignorin
 g entropic effects. This seminar will focus on the advancements made by Da
 sgupta and Herbert to make QM cluster enzyme models more realistic\, const
 raining atoms with a harmonic confining potential rather than fixing atomi
 c positions.1 I will present the theory behind these harmonic constraints\
 , as well as go over a test case from the paper.\n\n1) Saswata Dasgupta an
 d John M. Herbert\, J. Phys. Chem. B\, 2020\, 124 (7)\, 1137–1147. 4:00 
 pm
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