Tertiary contact formation rates in α-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 α-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.
[1]
William H. Press,et al.
Numerical Recipes in FORTRAN - The Art of Scientific Computing, 2nd Edition
,
1987
.
[2]
Charles L. Lawson,et al.
Solving least squares problems
,
1976,
Classics in applied mathematics.
[3]
John G. Kemeny,et al.
Finite Markov chains
,
1960
.
[4]
B. Fierz,et al.
Dynamics of Unfolded Polypeptide Chains
,
2005
.