Publications by authors named "Kristin Tyson"
Article Synopsis
- Tryptophan plays a key role in electron transfer and reducing oxidative damage in proteins, with varying electrochemical potentials influenced by its local hydrogen-bonding environment.
- The study investigates how mutations at position Phe110 affect the electrochemical properties of tryptophan at position 48, using techniques like X-ray diffraction and UV resonance Raman spectroscopy.
- Findings suggest that water molecules in the protein environment can enhance electrochemical potentials and reveal complex interactions involving hydrogen bonding and local polarity around tryptophan.
Fluorinated 5-hydroxytryptophans (F-5HOWs) were synthesized in gram scale quantities and incorporated into a β-hairpin peptide and the protein azurin. The redox-active F-5HOWs exhibit unique radical spectroscopic signatures that expand the function of as probes for biological electron transfer.
View Article and Find Full Text PDFTyrosine and tryptophan play critical roles in facilitating proton-coupled electron transfer (PCET) processes essential to life. The local protein environment is anticipated to modulate the thermodynamics of amino acid radicals to achieve controlled, unidirectional PCET. Herein, square-wave voltammetry was employed to investigate the electrostatic effects on the redox properties of tryptophan in two variants of the protein azurin.
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