| 000 | 04100nam a2200385 i 4500 | ||
|---|---|---|---|
| 999 |
_c393142 _d393142 _x1 |
||
| 001 | 393142 | ||
| 003 | ES-MaUEC | ||
| 005 | 20240314174332.0 | ||
| 006 | a|||| o|||| 00| 0 | ||
| 007 | cr nn 008mamaa | ||
| 008 | 100301s2002 xxua o |||| 0|eng d | ||
| 020 | _a9781592591831 | ||
| 024 | 7 |
_a10.1385/1592591833 _2doi |
|
| 040 |
_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC |
||
| 050 | 4 |
_aQP551 _b2002 EB |
|
| 245 | 0 | 0 |
_aCalcium-Binding Protein Protocols _nVolume 1, _pReviews and Case Studies _cedited by Hans J. Vogel |
| 250 | _a1st edition 2002 | ||
| 264 | 1 |
_aTotowa, NJ _bHumana Press _c2002 |
|
| 300 |
_a1 recurso en línea (XVI, 340 páginas) _b133 ilustraciones, 4 ilustraciones a color |
||
| 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 _v172 |
|
| 505 | 0 | _aand Reviews -- Calcium-Binding Proteins -- Calcium -- Crystal Structure of Calpain and Insights into Ca2+-Dependent Activation -- The Multifunctional S100 Protein Family -- Ca2+Binding to Proteins Containing ?-Carboxyglutamic Acid Residues -- The Caseins of Milk as Calcium-Binding Proteins -- Calcium-Binding Proteins: Case Studies -- Preparation of Recombinant Plant Calmodulin Isoforms -- Isolation of Recombinant CardiacTroponin C -- Skeletal Muscle Troponin C -- Purification of Recombinant Calbindin D9k -- S100 Proteins -- Cadherins -- ?-Lactalbumin and (Calcium-Binding) Lysozyme -- Recombinant Annexin II Tetramer -- Purification and Characterization of ALG-2 A Novel Apoptosis-Linked Ca2+-Binding Protein -- Crystallization and Structural Details of Ca2+-Induced Conformational Changes in the EF-Hand Domain VI of Calpain -- Neurocalcin -- Crystallization and Structure-Function of Calsequestrin -- Use of Fluorescence Resonance Energy Transfer to Monitor Ca2+-Triggered Membrane Docking of C2 Domains -- Ca2+-Binding Mode of the C2A-Domain of Synaptotagmin -- Study of Calcineurin Structure by Limited Proteolysis. | |
| 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 Studies and Volume 2: Methods and Techniques-Hans Vogel and a panel of leading researchers review the protein chemistry and behavior of this significant protein class, and provide a comprehensive collection of proven experimental techniques for their study both in vitro and in vivo. This first volume discusses the role of calcium in intracellular secondary messenger activation mechanisms, including unique aspects of calcium chemistry and its utilization in dairy proteins and blood clotting. Detailed case studies provide a wealth of valuable information about protein purification and characterization strategies, X-ray crystallography, and specific calcium-binding proteins and their modes of action. The second companion volume, Methods and Techniques, focuses on cutting-edge experimental methods for studying solution structure, stability, dynamics, calcium-binding properties, and biological activity of calcium-binding proteins in general. 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: _z9781617371356 |
| 776 | 0 | 8 |
_iPrinted edition: _z9780896036888 |
| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592591833 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
| 942 |
_2lcc _cLE |
||
| 998 |
_b01/2024 _dz _eb _zSI |
||