Reactions in enzymatic catalysis is still widely discussed. Of the conformational changes in the protein globule during chemical Of the functional groups in the enzyme’s active site. 1 That tremendous acceleration is explained mainly by theĭimensional organization of protein globule and the precise location Enzymes are unique protein machines, which accelerateĬhemical reactions up to 17 orders of magnitude. We believe that such remotely actuated systemsĬan find applications in advanced manufacturing, nanomedicine, andĪ well-researched area that is critical for mechanistic understanding Both the catalytic activityĪnd the protein structure of MNP-CT conjugates restored 3 h after In the random structures in LFMF, as shown by attenuated total reflectionįourier transformed infrared spectroscopy. Of the point of conjugation to MNPs, the CT secondary structure wasĪffected with nearly complete loss of α-helices and increase Or carboxylic groups, LFMF alters the Michaelis–Menten constantīut not the apparent catalytic constant k cat (= V max/ o). Consistent with this, in CT conjugated to MNPs by either amino Of the substrate-binding site but little if any changes in the catalytic To the CT globule by its amino or carboxylic groups causes shrinkage The MD simulation suggests that application of the stretching force The latter are functionalized by eitherĬarboxylic or amino group moieties to vary the points of enzyme attachment. Secondary structure to study α-chymotrypsin (CT) conjugated
(MD) and in vitro spectroscopic analysis of the enzyme kinetics and We apply in silico simulations by molecular dynamics In the catalytic activity of the non-heating low-frequency magneticįield (LFMF). To magnetic nanoparticles (MNPs) undergo changes
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