Elucidation of Prion Protein Conformational Changes Associated with Infectivity by Fluorescence Spectroscopy
Final rept. 15 May 2003 - 14 May 2007
MONTANA UNIV MISSOULA
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Steady state and lifetime fluorescence measurements were made on 12 single tryptophan mutants of recombinant hamster prion protein, using acrylamide as quencher. The fluorescent properties of tryptophan are known to be sensitive to the local protein environment, so they were measured for three forms of the protein the alpha-helical monomeric form the normal form, the octameric beta-oligomer, and the fibrillar state. The latter two are models of the diseased state. All mutants examined showed that upon conversion from the alpha-helical form to the beta sheet states, the tryptophan became more buriedless solvent exposed. The data support the structural model of prion amyloid put forth by Cobb and Surewicz, which shows in-register stacking of beta strands in the amyloid core.
- Atomic and Molecular Physics and Spectroscopy