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008			110414s2009 xxu| fo |||| 0|eng d
020			_a9781597453677
024	7		_a10.1007/978-1-59745-367-7 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP551 _b2009 EB
245	0	0	_aProtein Structure, Stability, and Interactions _cedited by John W. Shriver
250			_a1st edition 2009
264		1	_aTotowa, NJ _bHumana Press _c2009
300			_a1 recurso en línea (X, 360 páginas) _b135 ilustraciones
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 _v490
505	0		_aMicrocalorimetry of Proteins and Their Complexes -- Determining the Conformational Stability of a Protein Using Urea Denaturation Curves -- Defining the Stability of Multimeric Proteins -- Protein-Protein and Ligand-Protein Interactions Studied by Analytical Ultracentrifugation -- Monitoring Molecular Interactions by NMR -- Ligand-Binding Interactions and Stability -- A Method for Direct Measurement of Protein Stability In Vivo -- Quantifying the Roles of Water and Solutes (Denaturants, Osmolytes, and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Model -- Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions -- Defining the Role of Salt Bridges in Protein Stability -- Protein Stabilization by the Rational Design of Surface Charge-Charge Interactions -- NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange -- Single-Molecule Fluorescence Studies of Protein Folding -- Experimental Characterization of the Denatured State Ensemble of Proteins.
520			_aIn the areas of biochemistry and cell biology, characterizations of stability and molecular interactions call for a quantitative approach with a level of precision that matches the fine tuning of these interactions in a living cell. Supporting and up-dating previous Methods in Molecular Biology™ volumes, Protein Structure, Stability, and Interactions approaches its subject with a focus on theory and practical applications for both established methods as well as exciting new procedures. The volume presents an overview of many techniques currently used to study protein stability and interactions, including scanning and titration calorimetry, spectroscopic methods, high field NMR, and analytical ultracentrifugation. As a volume of the highly successful Methods in Molecular Biology™ series, this work provides the kind of detailed description and implementation advice that is crucial for getting optimal results. Cutting-edge and easy to reference, Protein Structure, Stability, and Interactions is an ideal guide for all scientists interested in biomolecular interactions.
988			_aSpringer_Protocols_2009
650		7	_2embne _9242917 _aProteínas _xAnálisis
776	0	8	_iPrinted edition: _z9781607610311
776	0	8	_iPrinted edition: _z9781617378553
776	0	8	_iPrinted edition: _z9781588299543
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-59745-367-7 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b11/2023 _dz _ean _zSI