title: Thermodynamic analysis of metal ion-induced protein assembly.
abstract: A large number of biological systems are regulated by metal ion-induced protein assembly. This phenomenon can play a critical role in governing protein function and triggering downstream biological responses. We discuss the basic thermodynamic principles of linked equilibria that pertain to metal ion-induced dimerization and describe experimental approaches useful for studying such systems. The most informative techniques for studying these systems are sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation, although a wide range of other spectroscopic, chromatographic, or qualitative approaches can provide a wealth of useful information. These experimental procedures are illustrated with examples from two systems currently under study: zinc-induced assembly of a staphylococcal protein responsible for intercellular adhesion in bacterial biofilms and calcium-induced dimerization of a human nucleotidase.
authors.affiliation: Department of Molecular Genetics, Biochemistry & Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA.
authors.forename: Andrew B
authors.initials: AB
authors.lastname: Herr
authors.forename: Deborah G
authors.initials: DG
authors.lastname: Conrady
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D018441:Biofilms / Q000254:growth & development; D002118:Calcium / Q000378:metabolism*; D005470:Fluorometry; D006801:Humans; D009708:Nucleotidases / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D055503:Protein Multimerization; D013212:Staphylococcus epidermidis / Q000254:growth & development / Q000502:physiology; D013816:Thermodynamics; D014461:Ultracentrifugation; D015032:Zinc / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D009708:Nucleotidases; C526909:calcium-activated nucleotidase, human; D015032:Zinc; D002118:Calcium