This repository contains a molecular dynamics trajectory of the trp_cage miniprotein (PDB: 1L2Y), a 20-residue engineered protein that folds rapidly and serves as an important model system for protein
Fast-atom bombardment mass spectrometry was used to follow the time course of disulfide bond formation during in vitro refolding of recombinant human macrophage-colony-stimulating factor. The content
The essential chaperonin TRiC/CCT mediates protein folding in cooperation with the co-chaperone prefoldin (PFD). As shown in vitro, the cylindrical TRiC complex facilitates folding through ATP-regulat
Unfolding and Refolding Rips Dataset of the mechanical unfolding of ARC-L1-ARC protein. Paper Title: The Energy Cost of Polypeptide Knot Formation and its Folding Consequences