Using Go-Model Simulation to Capture the Complexity of the $\alpha$-Spectrin

POSTER

Abstract

The protein $\alpha$-spectrin is composed of a repeating helical structure that can be separated into three domains named R15, R16, and R17. Although each domain is highly homologous, the folding mechanism and kinetics are distinct. Most strikingly, the folding time of R15 is three orders of magnitude larger than R16, with R17 being the slowest. The origin of this wide range of rates has been attributed to roughness in energy landscapes and internal friction. We show that a simple analytic model is able to capture the subtleties of folding each domain, despite their structural similarities. In particular, our model predicts the increasing complexity from R15 to the R16 and R17 domains which explains the kinetic trends seen in experiments.

Authors

  • Daniel Gavazzi

    Kent State University

  • Frazier Baker

    Youngstown State University, Kent State University, Liquid Crystal Institute, Kent State University, Department of Biological Sciences, Kent State University, Department of Physics, Department of Chemistry and Biochemistry, Kent State University, Stony Brook Univ, Ohio Univ, Institute for Advanced Simulation, Institut fur Kernphysik, and Julich Center, Bowling Green State University, Dept. of Physics, Hiram College, Ohio State Univ - Columbus, Kent State University, Psychology Dept, Cleveland State University, Physics Dept, Cleveland State University, Chemical Physics Interdisciplinary Program and Liquid Crystal Institute, Kent State University, Kent, OH 44242-0001, USA, Univ of Konstanz, Univ College London, NIST, Hiroshima Univ, KIT, Missouri University of Science and Technology, University of California, San Diego, Georgia Institute of Technology, KSU, SKKU, Lock Haven Univ, Massachusetts General Hospital, University of Science and Technology of China, Yale University, Shanghai Institute of Microsystem and Information Technology, CAS, Nanjing University, Liquid Crystal Institute and Chemical Physics Interdisciplinary Program, Kent State University, Kent, OH 44242, USA, Department of Physics, Kent State University, Kent OH 44242, Department of Electro-Optic Engineering Ilse Katz Institute for Nanoscale Science and Technology Ben Gurion University, Beer Sheva 84105, Israel, Ohio University Zanesville