Download e-book for iPad: Calcium-Binding Proteins and RAGE: From Structural Basics to by Sonal Srikanth, Yousang Gwack (auth.), Claus W. Heizmann

By Sonal Srikanth, Yousang Gwack (auth.), Claus W. Heizmann (eds.)

ISBN-10: 1627032290

ISBN-13: 9781627032292

ISBN-10: 1627032304

ISBN-13: 9781627032308

Amajor course in scientific examine resulting in scientific purposes goals the legislation of intracellular calcium and a number of the human illnesses linked to an altered homeostasis of this international moment messenger. those illnesses contain, for instance: cardiomyopathy, irritation, mind problems, diabetes and melanoma. In Calcium-Binding Proteins and RAGE:from Structural fundamentals to ClinicalApplications,expert researchers within the box aspect a number of the equipment that are now prevalent to review calcium binding proteins. those equipment and strategies, corresponding to calcium-measurements, screening tools, medical chemistry, and remedy, are commonly appropriate to many different parts of simple and scientific learn in addition to to diagnostics. Written within the hugely profitable Methods in Molecular Biology™ sequence structure, chapters comprise introductions to their respective subject matters, lists of the mandatory fabrics and reagents, step by step, with ease reproducible laboratory protocols, and key tips about troubleshooting and averting recognized pitfalls.

Authoritative and practical,Calcium-Binding Proteins and RAGE:from Structural fundamentals to ClinicalApplications underlines the diagnostic and medical value of this relatives of proteins in human ailments and as drug targets.

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Milos M, Schaer J-J, Comte M, Cox JA (1986) Calcium-proton and calcium-magnesium antagonism in calmodulin. Biochemistry 25:6279–6287 5. Heizmann CW, Cox JA (1998) New perspectives on S100 proteins: a multifunctional Ca2+-, Zn2+- and Cu2+-binding protein family. Biometals 11:383–397 6. Mamar-Bachi A, Cox JA (1987) Quantitative analysis of the free energy coupling in the system calmodulin, calcium, smooth muscle myosin light chain kinase. Cell Calcium 8: 473–482 7. Cox JA (1988) Interactive properties of calmodulin.

In the monomer Zn2+ binds to a site different from the Ca2+ site, likely opposite to the two Ca2+ sites. In contrast Cu2+ seems to use the Ca2+ ligands. The secondary structure does not change upon binding of metal ions, but the microenvironment of the Tyr changes upon binding of Ca2+, but not of Zn2+. S100A13 is expressed in different tissues, but often in a cell type-specific manner in these tissues; it seems to function in exocytosis since it is a target of anti-allergic drugs (21, 22). 3). Mg2+ (2 mM) has no effect on 2 Divalent Cation-Protein Interactions 19 the Ca2+-binding isotherm.

But quantitative information, leading to the evaluation of the physiological significance of Ca2+-binding to a protein, cannot be gathered by these methods. This section deals with the four most common methods to determine Ca2+-binding isotherms. 1. A. Cox Por 3). In practice, aliquots of a protein solution (20–100 mM of binding sites) are equilibrated against a series of buffers of increasing ion (Ca2+) concentrations. At the end the concentrations of protein and of total ligand are measured in both compartments.

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Calcium-Binding Proteins and RAGE: From Structural Basics to Clinical Applications by Sonal Srikanth, Yousang Gwack (auth.), Claus W. Heizmann (eds.)

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