Protein Folding

Protein folding is driven by the minimization of Gibbs free energy (ΔG), where the native state represents the global th...

Protein folding is driven by the thermodynamic necessity to minimize free energy, a process conceptualized as the foldin...

Molecular chaperones ensure proteins achieve their functional 3D conformations without aggregating. Key systems include ...

Co-translational folding describes the process where a nascent polypeptide begins acquiring its 3D structure while still...

The ribosomal exit tunnel is a 100Å channel through which nascent polypeptides emerge. Its geometry permits α-helix form...

The molten globule is a compact folding intermediate with native-like secondary structure but a fluid, dynamic tertiary ...

CMA is a selective autophagy pathway where cytosolic proteins containing KFERQ-like motifs are recognized by Hsc70, deli...