A new folding paradigm for repeat proteins.
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.
Kajander
Tommi
T
Department of Molecular Biophysics and Biochemistry, Physics and Applied Physics, and Chemistry, Yale University, New Haven, Connecticut 06520, USA.
Cortajarena
Aitziber L
AL
Main
Ewan R G
ER
Mochrie
Simon G J
SG
Regan
Lynne
L
D020816:Amino Acid Motifs; D008956:Models, Chemical; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins