Single-molecule force spectroscopy (SMFS) is an emerging tool to investigate mechanical
properties of biomolecules and their responses to mechanical forces, and one of the most …

Unfolding and refolding of multidomain proteins under force have yet to be recognized as a
major mechanism of function for proteins in vivo. In this review, we discuss the inherent …

Binding-induced mechanical stabilization plays key roles in proteins involved in muscle
contraction, cellular mechanotransduction, or bacterial adhesion. Because of the vector …

Outer mitochondrial membrane protein mitoNEET (mNT) is a target of the type 2 diabetes
drug pioglitazone. It contains a labile Fe2S2 (His) 1 (Cys) 3 metal cluster with a single Fe–N …

The mitochondrial outer membrane protein, mitoNEET (mNT), is an iron–sulfur protein
containing an Fe2S2 (His) 1 (Cys) 3 cluster with a unique single Fe–N bond. Previous …

Sortase is one of the most widely used enzymes for covalent protein conjugation that links
protein and protein/small molecules together in a site-specific way. It typically recognizes the …

Copper/zinc superoxide dismutase (SOD) is a homodimeric metalloenzyme that has been
extensively studied as a benchmark for structure–function relationships in proteins, in …

α3D is a de novo designed three-helix bundle protein. Like most naturally occurring helical
proteins, it is mechanically labile with an unfolding force of< 15 pN, revealed by atomic force …

High-potential iron–sulfur proteins (HiPIPs) are an important class of metalloproteins with a
[4Fe–4S] cluster coordinated by four cysteine residues. Distinct from other iron–sulfur …

Thanks to the binding of various metal ions, metalloprotein plays an essential role in many
different biological processes and represents an indispensable protein subgroup. Thus, the …