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008			100301s2002 xxu| fo |||| 0|eng d
020			_a9781592591848
024	7		_a10.1385/1592591841 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQH345 _b2002 EB
245	0	0	_aCalcium-Binding Protein Protocols _nVolume 2, _pMethods and Techniques _cedited by Hans J. Vogel
250			_a1st edition 2002
264		1	_aTotowa, NJ _bHumana Press _c2002
300			_a1 recurso en línea (XVII, 415 páginas)
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Biology _x1940-6029 _v173
505	0		_aMethods and Techniques to Study -- Quantitative Analysis of Ca2+-Binding by Flow Dialysis -- Calcium Binding to Proteins Studied via Competition with Chromophoric Chelators -- Deconvolution of Calcium-Binding Curves -- Absorption and Circular Dichroism Spectroscopy -- Fourier Transform Infrared Spectroscopy of Calcium-Binding Proteins -- Steady-State Fluorescence Spectroscopy -- Fluorescence Methods for Measuring Calcium Affinity and Calcium Exchange with Proteins -- Surface Plasmon Resonance of Calcium-Binding Proteins -- Differential Scanning Calorimetry -- Isothermal Titration Calorimetry -- Multiangle Laser Light Scattering and Sedimentation Equilibrium -- Small-Angle Solution Scattering Reveals Information on Conformational Dynamics in Calcium-Binding Proteins and in their Interactions with Regulatory Targets -- Investigation of Calcium-Binding Proteins Using Electrospray Ionization Mass Spectrometry -- Synthetic Calcium-Binding Peptides -- Proteolytic Fragments of Calcium-Binding Proteins -- Electron Magnetic Resonance Studies of Calcium-Binding Proteins -- Cadmium-113 and Lead-207 NMR Spectroscopic Studies of Calcium-Binding Proteins -- Calcium-43 NMR of Calcium-Binding Proteins -- Exploring Familial Relationships Using Multiple Sequence Alignment -- Structure Determination by NMR -- Protein Structure Calculation from NMR Data -- Shape and Dynamics of a Calcium-Binding Protein Investigated by Nitrogen-15 NMR Relaxation -- The Use of Dipolar Couplings for the Structure Refinement of a Pair of Calcium-Binding EGF Domains -- Vector Geometry Mapping -- Use of Calmodulin Antagonists and S-100 Protein Interacting Drugs for Affinity Chromatography -- Enzymatic Assays to Compare Calmodulin Isoforms, Mutants, and Chimeras -- Gene Expression inTransfected Cells -- Monitoring the Intracellular Free Ca2+-Calmodulin Concentration with Genetically-Encoded Fluorescent Indicator Proteins -- Studying the Spatial Distribution of Ca2+-Binding Proteins.
520			_aCalcium-binding proteins play an important role in a variety of vital biological processes, ranging from blood clotting and signal transduction in cells, to attaching proteins to membranes and serving as an integral source of calcium. In Calcium-Binding Protocols- Volume 1: Reviews and Case Histories and Volume 2: Methods and Techniques-Hans Vogel and a panel of leading researchers review the protein chemistry and behavior of this significant class proteins, and provide a comprehensive collection of proven experimental techniques for studying it both in vitro and in vivo. This second volume focuses on cutting-edge experimental techniques for studying the solution structure, stability, dynamics, calcium-binding properties, and biological activity of calcium-binding protein in general. In addition to enzymatic assays and more routine spectroscopic and protein chemistry techniques, there are also NMR approaches, thermodynamic analyses, kinetic measurements such as surface plasmon resonance, strategies for amino acid sequence alignments, and fluorescence methods to study the distribution of calcium and calcium-binding proteins in cells. The first companion volume, Reviews and Case Histories sets the stage for this volume by introducing the various classes of intra- and extracellular calcium-binding proteins and their mode of action. Comprehensive and highly practical, the two volumes of Calcium-Binding Protocols provide experimental and clinical biologists with a host of advanced experimental methods that can be applied successfully to the study of both existing and newly discovered members of this critically important class of proteins.
988			_aSpringer_Protocols_2002
650		7	_2embne _9139861 _aProteínas
776	0	8	_iPrinted edition: _z9781617371363
776	0	8	_iPrinted edition: _z9780896036895
776	0	8	_iPrinted edition: _z9781489939104
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592591841 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b10/2023 _dz _ean _zSI