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Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein.
A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.
Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system.
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy.
Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase.
The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.