Finite size effects on thermal denaturation of globular proteins

Phys Rev Lett. 2004 Dec 31;93(26 Pt 1):268107. doi: 10.1103/PhysRevLett.93.268107. Epub 2004 Dec 21.

Abstract

Finite size effects on the cooperative thermal denaturation of proteins are considered. A dimensionless measure of cooperativity, Omegac, scales as Nzeta, where N is the number of amino acids. Surprisingly, we find that zeta is universal with zeta=1+gamma, where the exponent gamma characterizes the divergence of the susceptibility for a self-avoiding walk. Our lattice model simulations and experimental data are consistent with the theory. Our finding rationalizes the marginal stability of proteins and substantiates the earlier predictions that the efficient folding of two-state proteins requires TF approximately Ttheta, where Ttheta and TF are the collapse and folding transition temperatures, respectively.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Computer Simulation
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Phase Transition
  • Protein Denaturation*
  • Protein Folding*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Structure-Activity Relationship
  • Temperature*

Substances

  • Proteins