About
Alvan Hengge serves as a Professor in the Chemistry and Biochemistry Department at Utah State University's College of Arts & Sciences, with his office located in WIDT 343 at 0300 Old Main Hill, Logan, UT 84322.
His research program centers on enzymatic mechanisms, particularly the structural dynamics and catalytic functions of protein phosphatases. Key investigations include the role of conformational motions (e.g., WPD-loop dynamics) in pH-dependent catalysis, evolutionary constraints on nucleotide-binding proteins, and physical organic chemistry of phosphoryl/sulfuryl transfer reactions. This work integrates kinetic isotope effects, NMR spectroscopy, computational modeling, and protein engineering to dissect enzyme function at atomic resolution.
Analysis of his 2019–2025 publications reveals a cohesive research trajectory focused on protein tyrosine phosphatases, with recurring themes in loop dynamics, catalytic promiscuity, and evolutionary biochemistry. Notable contributions include elucidating dual-acid functionality in archaeal phosphatases, engineering thermostable variants, and defining transition-state interactions in promiscuous enzymes like arylsulfatases. His work bridges fundamental mechanistic biochemistry with potential applications in inhibitor design.
No scientific awards were documented in the available materials.
Details regarding student advising, research grants, or laboratory infrastructure were not provided in the source data.
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