Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.

@article{Ulmer2005ComparisonOS,
  title={Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.},
  author={Tobias S Ulmer and Adriaan Bax},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 52},
  pages={43179-87}
}
Three point mutations (A30P, E46K, and A53T) as well as gene triplication genetically link the 140-residue protein alpha-synuclein (aS) to the development of Parkinson disease. Here, the structure and dynamics of micelle-bound aS(A30P) and aS(A53T) are described and compared with wild-type aS, in addition to describing the aS-micelle interaction. A53T is sensed only by directly adjacent residues and leaves the backbone structure and dynamics indistinguishable from the wild type. A30P interrupts… CONTINUE READING

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