title: GB1 is not a two-state folder: identification and characterization of an on-pathway intermediate.
abstract: The folding pathway of the small α/β protein GB1 has been extensively studied during the past two decades using both theoretical and experimental approaches. These studies provided a consensus view that the protein folds in a two-state manner. Here, we reassessed the folding of GB1, both by experiments and simulations, and detected the presence of an on-pathway intermediate. This intermediate has eluded earlier experimental characterization and is distinct from the collapsed state previously identified using ultrarapid mixing. Failure to identify the presence of an intermediate affects some of the conclusions that have been drawn for GB1, a popular model for protein folding studies.
authors: Istituto Pasteur-Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università di Roma "La Sapienza", Rome, Italy.
authors: Angela
authors: A
authors: Morrone
authors: Rajanish
authors: R
authors: Giri
authors: Rudesh D
authors: RD
authors: Toofanny
authors: Carlo
authors: C
authors: Travaglini-Allocatelli
authors: Maurizio
authors: M
authors: Brunori
authors: Valerie
authors: V
authors: Daggett
authors: Stefano
authors: S
authors: Gianni
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus