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008			130217s2013 xxua o |||| 0|eng d
020			_a9781627032759
024	7		_a10.1007/978-1-62703-275-9 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP751 _b2013 EB
245	0	0	_aLipid-Protein Interactions : _bMethods and Protocols _cedited by Jörg H. Kleinschmidt
250			_a1st edition 2013
264		1	_aTotowa, NJ _bHumana Press _c2013
300			_a1 recurso en línea (X, 464 páginas) _b107 ilustraciones, 56 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 _v974
505	0		_aQuartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions -- Surface Plasmon Resonance for Measuring Interactions of Proteins with Lipid Membranes -- Probing the Thermodynamics of Protein-Lipid Interactions by Isothermal Titration Calorimetry -- Differential Scanning Calorimetry of Protein-Lipid Interactions -- Atomic Force Microscopy and Spectroscopy to Probe Single Membrane Proteins in Lipid Bilayers -- Optimized Negative-Staining Protocol for Lipid-Protein Interactions Investigated by Electron Microscopy -- Examining the Protein-Lipid Complexes using Neutron Scattering -- Circular-Dichroism and Synchrotron-Radiation Circular-Dichroism Spectroscopy as Tools to Monitor Protein Structure in a Lipid Environment -- Structural Characterization of Membrane Proteins and Peptides by FTIR and ATR-FTIR Spectroscopy -- Förster Resonance Energy Transfer as a Tool for Quantification of Protein-Lipid Selectivity -- A Guide to Tracking Single Transmembrane Proteins in Supported Lipid Bilayers -- Fluorescence Correlation Spectroscopy to Examine Protein Lipid Interactions in Membranes -- Analyzing Transmembrane Protein and Hydrophobic Helix Topography by Dual Fluorescence Quenching -- Studying Lipid-Protein Interactions with Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids -- EPR Techniques to Probe Insertion and Conformation of Spin-Labeled Proteins in Lipid Bilayers -- Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions -- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment -- Nanodiscs as a New Tool to Examine Lipid-Protein Interactions -- The Simulation Approach to Lipid-Protein Interactions.
520			_aBiological membranes are the essential structuring elements of all living cells. Many enzymatic reactions take place at the membrane-water interface. To gain detailed insight into membrane properties, it is therefore of great importance to understand the complex nature of the interactions of membrane proteins with lipids. Lipid-Protein Interactions: Methods and Protocols provides a selection of protocols to examine protein-lipid interactions, membrane and membrane protein structure, how membrane proteins affect lipids and how they are in turn affected by the lipid bilayer and lipid properties. The methods described here are all actively used, complementary, and necessary to obtain comprehensive information about membrane structure and function. They include label-free approaches, imaging techniques and spectroscopic methodologies. Written in the successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and easily accessible, Lipid-Protein Interactions: Methods and Protocols seeks to serve both professional and novices with its wide range of the methods frequently used in this area of research.
988			_aSpringer_Protocols_2013
650		7	_2embne _9142933 _aLípidos _vManuales de laboratorio
776	0	8	_iPrinted edition: _z9781627032742
776	0	8	_iPrinted edition: _z9781627032766
776	0	8	_iPrinted edition: _z9781493962631
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-62703-275-9 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b12/2023 _dz _eb _zSI