title: A new folding paradigm for repeat proteins.
abstract: The folding/unfolding transitions of a series of designed consensus tetratricopeptide repeat proteins are quantitatively described by the classical one-dimensional Ising model, which thus represents a new folding paradigm for repeat proteins. Moreover, for the first time for any protein, a theoretical model predicts the folding/unfolding transition midpoint and the width of the transition.
authors: Department of Molecular Biophysics and Biochemistry, Physics and Applied Physics, and Chemistry, Yale University, New Haven, Connecticut 06520, USA.
authors: Tommi
authors: T
authors: Kajander
authors: Aitziber L
authors: AL
authors: Cortajarena
authors: Ewan R G
authors: ER
authors: Main
authors: Simon G J
authors: SG
authors: Mochrie
authors: Lynne
authors: L
authors: Regan
mesh_terms: D020816:Amino Acid Motifs; D008956:Models, Chemical; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins