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 …

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 …

The annexin fold consists of four 70-residue domains with markedly homologous sequences
and nearly identical structures. Each domain contains five helices designated A to E …

Annexins are excellent models for studying the folding mechanisms of multidomain proteins
because they have four–eight homologous helical domains with low identity in sequence but …

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 …

Annexins comprise a multigene family of Ca2+ and phospholipid-binding proteins. They
consist of a conserved C-terminal or core domain that confers Ca2+-dependent …

In 1993, Huber and co-workers published the structure of an N-terminally truncated version
of human annexin A1 lacking the first 32 amino acid residues (PDB code: 1AIN). In 2001, we …

Revised Manuscript Received July 26, 1995® abstract: A 21-residue peptide,
P1AQFD5ADELR10AAMKG15LGTDE20D, corresponding to the (helix A)-loop motif of the …

A model of domain II of annexin I has been built by homology modelling using an annexin V
crystal structure as a template. The method used is based on that of Summers and Karplus …

Abstract Two-dimensional (2-D) crystals of annexin V, grown by specific binding to
phosphatidylserine-containing planar lipid films, were studied by electron image analysis …