title: Unfolding proteins in an external field: can we always observe the intermediate states?
abstract: A protein molecule under the stress of an external denaturing force acting on a terminal end or on the entire molecule is expected to unfold, possibly through a few intermediate stages depending on the magnitude of the denaturing force. We have investigated two protein minimal models under various types of denaturing force fields using the collision molecular-dynamics simulation, in order to critically examine the relationship between the folding pathways observed in different protein denaturing experiments.
authors.affiliation: Department of Physics, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1.
authors.forename: Alexander S
authors.initials: AS
authors.lastname: Lemak
authors.forename: James R
authors.initials: JR
authors.lastname: Lepock
authors.forename: Jeff Z Y
authors.initials: JZ
authors.lastname: Chen
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D006358:Hot Temperature; D007700:Kinetics; D008962:Models, Theoretical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature