The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions

Investigating Protein Folding and Function by Manipulating Rare and Partially-Folded Conformations

Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.

Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins

Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins

Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR

Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.

Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein.

Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.

A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.

The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions

Investigating Protein Folding and Function by Manipulating Rare and Partially-Folded Conformations

Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.

Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins

Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins

Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR

Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.

Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein.

Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.

A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.

Autonomously Folding Protein Fragments Reveal Differences in the Energy Landscapes of Homologous RNases H

The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions

Investigating Protein Folding and Function by Manipulating Rare and Partially-Folded Conformations

Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.

Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins

Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins

Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR

Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.

Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein.

Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.

A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.

Autonomously Folding Protein Fragments Reveal Differences in the Energy Landscapes of Homologous RNases H