Protein folding – simplicity in complexity

Authors

  • M.M. Lin,

    1. Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA
    Search for more papers by this author
  • A.H. Zewail

    Corresponding author
    1. Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA
    • Physical Biology Center for Ultrafast Science and Technology, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA
    Search for more papers by this author
    • Phone: (626) 395-2611, Fax: (626) 792-8456


Abstract

Understanding and predicting protein folding would elucidate how misfolded proteins cause aggregation and amyloid formation, for example in Alzheimer's disease. Despite the seemingly bewildering complexity of protein biology, simple analytic models can still capture the basic physics and predict the fundamental limits for protein domain size and folding speed.

Ancillary