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Simulations as analytical tools to understand protein aggregation and predict amyloid conformation

  1. Author:
    Ma, B. Y.
    Nussinov, R.

  2. Author Address

    NCI, Basic Res Program, SAIC Frederick Inc, Ctr Canc Res, Frederick, MD 21702 USA. Tel Aviv Univ, Sackler Sch Med, Sackler Inst Mol Med, Dept Human Genet & Mol Med, IL-69978 Tel Aviv, Israel.;Nussinov, R, NCI, Basic Res Program, SAIC Frederick Inc, Ctr Canc Res, Frederick, MD 21702 USA.;ruthn@ncifcrf.gov
    1. Year: 2006
    2. Date: Oct
  2. Journal: Current Opinion in Chemical Biology
    1. 10
    2. 5
    3. Pages: 445-452
  4. Type of Article: Review
  5. ISSN: 1367-5931
  1. Abstract:

    Computational tools are increasingly being applied to solve the protein aggregation problem, providing insight into amyloid structures and aggregation mechanisms. The paradigm of A beta amyloid structure elucidation provides an example of an innovative experimental design and endeavor, echoing the computational testing of possible molecular associations, all reflected in the current Ma-Nussinov-Tycko model of the A beta amyloid. Simulations have shown that dimer formation can lock some misfolded conformations, and catalyze the shift of the equilibrium away from the native state. In most cases, a stable amyloid seed requires at least two-layered beta-sheets with properly registered side-chains. Under kinetic control, the final protein aggregations are the outcome of maximizing the van der Waals interactions between side chains and backbone hydrogen bonds.

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External Sources

  1. View record in Web of Science®
  2. WOS: 000241652200010

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