title: Analysis of PIN1 WW domain through a simple statistical mechanics model.
abstract: We have applied a simple statistical mechanics Go-like model to the analysis of the PIN1 WW domain, resorting to mean field and Monte Carlo techniques to characterize its thermodynamics, and comparing the results with the wealth of available experimental data. PIN1 WW domain is a 39-residue protein fragment which folds on an antiparallel beta-sheet, thus representing an interesting model system to study the behavior of these secondary structure elements. Results show that the model correctly reproduces the two-state behavior of the protein, and also the trends of the experimental phi(T) values. Moreover, there is a good agreement between Monte Carlo results and the mean field ones, which can be obtained with a substantially smaller computational effort.
authors.affiliation: Instituto BIFI, Universidad de Zaragoza, c/ Corona de Aragón 42, E-50009 Zaragoza, Spain. pier@unizar.es
authors.forename: Pierpaolo
authors.initials: P
authors.lastname: Bruscolini
authors.forename: Fabio
authors.initials: F
authors.lastname: Cecconi
mesh_terms: D015233:Models, Statistical; D009010:Monte Carlo Method; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013696:Temperature; D013816:Thermodynamics
chemical_list: D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase