Annexins are Ca2+ and phospholipid binding proteins forming an evolutionary conserved
multigene family with members of the family being expressed throughout animal and plant …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

A new strategy is described for the production of peptides enriched with stable isotopes.
Peptides of interest are expressed in Escherichia coli (E. coli) cells as recombinant fusion …

A spectral density model based on a truncated lorentzian distribution of correlation times is
used to analyze the nanosecond time‐scale dynamics of the partially unfolded domain 2 of …

The progression of aggressive cancer occurs via angiogenesis and metastasis makes these
processes important targets for the development of anti-cancer agents. However, recent …

The isolated D2 domain of annexin I is unable to adopt a tertiary fold but exhibits both native
and non-native residual structures. It thus constitutes an attractive model for the investigation …

Annexins (Anxs) are a family of highly homologous proteins that bind and aggregate lipid
vesicles in the presence of calcium. All members of the family contain a variable N-terminus …

The four∼ 75-residue domains (repeats) that constitute the annexin core structure all
possess an identical five-α-helix bundle topology, but the physico-chemical properties of the …

In the context of exploring the relationship between sequence and folding pathways, the
multi-domain proteins of the annexin family constitute very attractive models. They are …

Proteins of the annexin family constitute very attractive models because of their four∼ 70
residue domains, D1 to D4, exhibiting an identical topology comprising five helix segments …