Publications by authors named "Andrew F Philip"

Objective: The number of registered motorcycles in the United States has been steadily increasing, as have the number of motorcycle injuries and fatalities. The Midwest has the lowest incidence of helmet use in the country. Iowa in particular has no helmet law.

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PAS domains form a divergent protein superfamily with more than 20 000 members that perform a wide array of sensing and regulatory functions in all three domains of life. Only nine residues are well-conserved in PAS domains, with an Asn residue at the start of α-helix 3 showing the strongest conservation. The molecular functions of these nine conserved residues are unknown.

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The robustness of proteins against point mutations implies that only a small subset of residues determines functional properties. We test this prediction using photoactive yellow protein (PYP), a 125-residue prototype of the PER-ARNT-SIM (PAS) domain superfamily of signaling proteins. PAS domains are defined by a small number of conserved residues of unknown function.

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Article Synopsis
  • The study investigates how protein structure affects the absorption and emission spectra of chromophores in photoreceptors, particularly focusing on the role of a specific residue, residue 46, in photoactive yellow protein (PYP).
  • Research shows that changes in the absorbance spectra of mutant proteins suggest alterations in the width of the excited state energy surface (S(1)), rather than significant changes in the energy gap between the ground state (S(0)) and excited state (S(1)).
  • Findings indicate that while the position and width of absorbance spectra vary among mutants, fluorescence emission spectra remain mostly constant, highlighting that tuning effects are primarily due to changes in energy surface width.
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Protein-ligand interactions alter the properties of active site groups to achieve specific biological functions. The active site of photoactive yellow protein (PYP) provides a model system for studying such functional tuning. PYP is a small bacterial photoreceptor with photochemistry based on its p-coumaric acid (pCA) chromophore.

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