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Effect of the A30P mutation on the structural dynamics of micelle-bound αSynuclein released in water: a molecular dynamics study

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Abstract

Atomistic molecular dynamics simulation has been used to probe the effect of the A30P mutation on the structural dynamics of micelle-bound, helical αSynuclein when released in an aqueous environment. On the timescales simulated, the effect of the mutation on the secondary structure is restricted to local changes close to the mutation site in the N-terminal helical domain. The changes are transient, and all residues except Lys23 recover their initial structure. The local behavior due to the mutation gives rise to a global difference in the A30P mutant in the form of a permanent kink in the N-terminal helical domain.

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Acknowledgments

PC acknowledges CSIR for a Junior Research Fellowship. NS acknowledges funds from DST-India (fast track grant GAP280526), funds and computing resources from the Centre of Excellence in Scientific Computing at NCL, and computing resources from CDAC, Pune.

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Authors and Affiliations

  1. Physical Chemistry Division, National Chemical Laboratory, Pune, 411008, India

    Prathit Chatterjee & Neelanjana Sengupta

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  1. Prathit Chatterjee
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  2. Neelanjana Sengupta
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Correspondence to Neelanjana Sengupta.

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249_2012_803_MOESM1_ESM.docx

Electronic Supplementary Material: Supplementary material associated with this article consists of plots depicting evolution of persistence parameters for groups in N- and C-terminal domains; evolution of bend angles θ 1 and θ 2; and evolution of the hydrogen bonding network energy for N- and C-helices. (DOCX 2536 kb)

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Chatterjee, P., Sengupta, N. Effect of the A30P mutation on the structural dynamics of micelle-bound αSynuclein released in water: a molecular dynamics study. Eur Biophys J 41, 483–489 (2012). https://doi.org/10.1007/s00249-012-0803-y

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  • DOI: https://doi.org/10.1007/s00249-012-0803-y

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