Titlebook: Calcium-Binding Protein Protocols; Volume 2: Methods an Hans J. Vogel Book 2002 Humana Press 2002

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Small-Angle Solution Scattering Reveals Information on Conformational Dynamics in Calcium-Binding Prce of this scattering is related to the structure of the protein. For a solution of randomly oriented proteins, the scattering is concentrated in the vicinity of the direct beam, or zero-angle. Solution scattering is therefore often referred to as small-angle or low-angle scattering. Structural info

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Investigation of Calcium-Binding Proteins Using Electrospray Ionization Mass Spectrometrys that are used to characterize macromolecules. It is particularly suitable for studying proteins in their native state as the solvent conditions for transferring and ionizing protein molecules from solution to the gas phase can be similar to those used for characterizing proteins in solution. Follo

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Proteolytic Fragments of Calcium-Binding Proteinsifs. These motifs predominantly exist in pairs in these proteins, which is important for high-affinity, cooperative binding of Ca.ions. Separation of individual helix-loop-helix domains through proteolysis provides an ideal starting point to asses the importance of having these domains in pairs. In

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Cadmium-113 and Lead-207 NMR Spectroscopic Studies of Calcium-Binding Proteinsrotein. For calcium-binding proteins, the NMR active isotope .Ca is a quadrupolar (I = 7/2) nucleus that produces broad peaks when bound to a protein (.–.) Although much useful information can be gleaned from studies of this nucleus (.,.), it is impossible to resolve the signals for individual calci

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Book 2002 it modifies their biological activity or their stability. Because of its distinct che- cal properties calcium is uniquely suited to act as an on–off switch or as a light dimmer of biological activities. The two books entitled Calcium-Binding Protein Protocols (Volumes I and II) focus on modern expe

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Investigation of Calcium-Binding Proteins Using Electrospray Ionization Mass Spectrometrywing a study of myoglobin at the beginning of decade (.), there have been a number of reported ESI-MS studies of specific noncovalent protein-ligand complexes. A recent review by Loo provides a thorough list of ESI-MS studies of proteins interacting with metals, small molecules, peptides and proteins, and nucleic acids (.).

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