Simulation of two-dimensional streptavidin crystallization

Proteins. 2001 Jun 1;43(4):489-98. doi: 10.1002/prot.1060.

Abstract

We present lattice Monte Carlo simulations of the growth of streptavidin islands at a biotinylated lipid layer. The model employed takes into account attractive anisotropic lateral interactions between streptavidin tetramers. With a minimal set of interactions, we reproduce the formation of rectangular islands experimentally observed at pH > or = 9.0. Specifically, we analyze two scenarios of the island growth. First, if streptavidin is rapidly adsorbed at t = 0 (stepwise coverage change without ongoing adsorption), the average linear island size is found to grow according to the Lifshitz-Slyozov law, R proportional to t(1/3). Second, if the island growth occurs in parallel with streptavidin adsorption limited by diffusion in the solution, the Lifshitz-Slyozov law is also applicable, but only at the late stage, when the streptavidin coverage is appreciable.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Amino Acid Sequence
  • Anisotropy
  • Biotinylation
  • Computer Simulation*
  • Crystallization
  • Diffusion
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lipid Bilayers / chemistry
  • Models, Molecular
  • Monte Carlo Method
  • Protein Conformation
  • Streptavidin / chemistry*
  • Temperature
  • Time Factors

Substances

  • Lipid Bilayers
  • Streptavidin