Protein Folding Cooperativity: Basic Insights from Minimalist Models

Title: Protein Folding Cooperativity: Basic Insights from Minimalist Models

Volume: 12 Issue: 3

Author(s): Antonio F. Pereira de Araujo

Affiliation:

Keywords: lattice model, cooperativity, two-state transition, hydrophobicity, hydrogen bond, structural segregation, first-order phase transition

Abstract: Basic concepts about two-state, cooperative protein folding and its relation to first-order phase transitions are reviewed. Minimalist models capable of reproducing the required free energy barrier between folded and unfolded macroscopic states are described. A significantly more restrictive “calorimetric” criterion is also discussed, which is based on direct comparison between model and experimental heat capacities with additional assumptions about conformational enthalpy variation in the unfolded state.

Cite this article as:

de Araujo F. Pereira Antonio, Protein Folding Cooperativity: Basic Insights from Minimalist Models, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587101

DOI https://dx.doi.org/10.2174/0929866053587101	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305