title: Protein folding cooperativity: basic insights from minimalist models.
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.
authors.affiliation: Departamento de Biologia Celular Universidade de Brasília, Brasília-DF 70910-900, Brazil. aaraujo@unb.br
authors.forename: Antônio F Pereira
authors.initials: AF
authors.lastname: de Araújo
mesh_terms: D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D013997:Time Factors
chemical_list: D011506:Proteins