01739nas a2200205   4500008004500000020001400045245008900059210006900148260000800217300001400225490000800239520112900247653001501376100002101391700001701412700001901429700001601448700002001464856004901484       2020                        Engldsh    a0006-349500aLong Range Correlated Motions of TIM and their Possible Influence on Enzyme Function0 aLong Range Correlated Motions of TIM and their Possible Influenc  cFeb  a207A-207A0 v1183 a<p style="text-align: justify;">The alpha-beta barrel structure of triosephosphate isomerase (TIM) is possibly the most common among enzymes. In the case of TIM, structural dynamics are known to be essential to function. In particular the stabilization of the binding pocket by a phosphodianion “handle” of the substrate and the closing of catalytic site loops 6 and 7 over the substrate. Loop 6 moves by as much as 7 Angstroms with binding. Recently a mutant survey for human TIM (hsTIM) found kcat can change significantly for a single mutation distant from the catalytic site. Crystallographic measurements find no structural change with the mutation, suggesting a dynamical mechanism for the allosteric effect. Here we use Stationary Sample Anisotropic Terahertz Microscopy (SSATM) to measure the long-range intramolecular vibrations and determine if specific vibrations couple the allosteric and catalytic sites. SSATM isolated protein long-range structural vibrations based on the dominant displacement direction [1-4]. We examine if specific vibrational bands are associate with loop 6 and loop 7 flexibility.</p>10aBiophysics1 aMcKinney, J., A.1 aDeng, Y., T.1 aGeorge, D., K.1 aRichard, J.1 aMarkelz, A., G.  uhttps://markelz.physics.buffalo.edu/node/252