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

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书目名称Calcium-Binding Protein Protocols
副标题Volume 2: Methods an
编辑Hans J. Vogel
视频video
概述Includes supplementary material:
丛书名称Methods in Molecular Biology
图书封面Titlebook: Calcium-Binding Protein Protocols; Volume 2: Methods an Hans J. Vogel Book 2002 Humana Press 2002
描述Calcium plays an important role in a wide variety of biological processes. This divalent metal ion can bind to a large number of proteins; by doing so 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 experimental analyses and methodologies for the study of calcium-binding proteins. Both extracel- lar and intracellular calcium-binding proteins are discussed in detail. H- ever, proteins involved in calcium handling (e. g. , calcium pumps and calcium channels), fall outside of the scope of these two volumes. Also, calcium-bi- ing proteins involved in bone deposition will not be discussed, as this specific topic has been addressed previously. The focus of these two books is on studies of the calcium-binding proteins and their behavior in vitro and in vivo. The primary emphasis is on protein chemistry and biophysical methods. Many of the methods described will also be applicable to proteins that do not bind calcium. Calcium-Binding Protein Proto
出版日期Book 2002
版次1
doihttps://doi.org/10.1385/1592591841
isbn_softcover978-1-61737-136-3
isbn_ebook978-1-59259-184-8Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2002
The information of publication is updating

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Fluorescence Methods for Measuring Calcium Affinity and Calcium Exchange with Proteinsnd smooth muscle contraction, neurotransmission, cell proliferation, and division. Nature has designed hundreds of Ca.-binding proteins that sense the “Ca. signal” and transduce it into cellular action. Ca.-binding proteins are “tuned” to respond to these Ca.transients by virtue of their specific Ca
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Isothermal Titration Calorimetrynteracting systems. The method of choice for the direct measurements of energetics of protein-ligand interactions is the isothermal titration calorimetry (ITC) technique. The use of ITC to measure the binding of a macromolecule (in general, a protein) to its ligand (ion, peptide, another protein, DN
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Multiangle Laser Light Scattering and Sedimentation Equilibrium proteins and their interactions in solution under physiological conditions. Both techniques have undergone a resurgence as a result of the advent of recombinant technologies which has enabled the generation of reasonable quantities of biologically significant proteins that exist in vivo in small am
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