Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 111, Issue 8, Pages 2107-2112Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp068604y
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Funding
- NIDDK NIH HHS [R01 DK019038, R37 DK019038, DK19038] Funding Source: Medline
- NIGMS NIH HHS [R01 GM068461, R01 GM068461-05, GM068461] Funding Source: Medline
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Tertiary contact formation rates in alpha-synuclein, an intrinsically disordered polypeptide implicated in Parkinson's disease, have been determined from measurements of diffusion-limited electron-transfer kinetics between triplet-excited tryptophan:3-nitrotyrosine pairs separated by 10, 12, 55, and 90 residues. Calculations based on a Markovian lattice model developed to describe intrachain diffusion dynamics for a disordered polypeptide give contact quenching rates for various loop sizes ranging from 6 to 48 that are in reasonable agreement with experimentally determined values for small loops (10-20 residues). Contrary to expectations, measured contact rates in alpha-synuclein do not continue to decrease as the loop size increases (>= 35 residues), and substantial deviations from calculated rates are found for the pairs W4-Y94, Y39-W94, and W4-Y136. The contact rates for these large loops indicate much shorter average donor-acceptor separations than expected for a random polymer.
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