Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems

The serpins constitute a superfamily of proteins that fold into a conserved tertiary structure and employ a sophisticated, irreversible suicide-mechanism of inhibition. More than 6000 serpins have been identified, occurring in all three forms of the life - the eukaryotes, the prokaryotes and the archea. Vertebrate serpins can be conveniently classified into six groups (V1 - V6), based on three independent biological features - gene organization, diagnostic amino acid sites and rare indels. In the present work, the phylogenetic relationships of serpins from Nematostella vectensis, Strongylocentrotus purpuratus, Ciona intestinalis, and selected vertebrates were investigated. With some deviations, all vertebrate serpin genes fit into one of the six exon/intron gene classes previously identified, dating the existence and maintenance of these gene organizations before or close to the divergence of fishes. Multiple intron acquisition events have occurred in selected serpins during diversification of a lineage of actinopterygian fishes, whose genome underwent compaction. The novel introns were acquired within a limited time interval (on an evolutionary timescale) and only in these fishes.

Proteases refer to a group of enzymes whose catalytic function is to hydrolyse (cleavage) peptide bonds of proteins. Proteases occur naturally in all organisms and are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades. In this book, the authors discuss the maturation and stabilisation mechanisms of two hyperthermostable subtilisin-like serine proteases from thermococcus kodakarensis; serine protease-related innate immunity; fungal and bacterial serine proteases; and the physiological function and pathology of neurosin/kallikrein 6 in the central nervous system.

Proteases refer to a group of enzymes whose catalytic function is to hydrolyze(cleavage) peptide bonds of proteins. Proteases occur naturally in all organisms and are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades. In this book, the authors discuss the maturation and stabilization mechanisms of two hyperthermostable subtilisin-like serine proteases from thermococcus kodakarensis; serine protease-related innate immunity; fungal and bacterial serine proteases; and the physiological function and pathology of neurosin/kallikrein 6 in the central nervous system.

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.