@misc{9230643,
  abstract     = {{This work studied a metal fluoride transition state analogue (TSA) complex of β-phosphoglucomutase (βPGM), a phosphoryl transfer enzyme catalysing the interconversion of glucose-6-phosphate (G6P) and glucose-1-phosphate (G1P), and its P146A and A136N mutants using advanced NMR spectroscopy methods. Conformational exchange rates of βPGM:MgF3–:G6P TSA complex were extracted at a grid of temperatures (278, 288, and 298 K) and pressures (1-2000 bar) using 2D 19F Nuclear Overhauser Effect (NOE) spectroscopy. The volume, entropy, and enthalpy of activation for this conformational exchange process were quantified through a thermodynamic global fit of exchange rates. The global fit yields ∆V‡ minor→major = 38±1 mL/mol and ∆V‡ major→minor = 8±1 mL/moL, giving a net reaction volume of ∆V0 = 30 mL mol−1 in the forward direction consistent with structural reorganization and partial unfolding. 15N T2 CPMG relaxation dispersion (RD) experiments across different pressures established key residues involved in the conformational exchange, which are situated in the active site. This ties together the global conformational exchange process of βPGM:MgF3–:G6P TSA and local conformational exchange processes within the protein.}},
  author       = {{Iman, Hilya}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{Activation volumes and structural reorganisation in the conformational exchange of β-phosphoglucomutase transition state analogue complexes}},
  year         = {{2026}},
}