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007			cr nn 008mamaa
008			110628s2011 xxu| s |||| 0|eng d
020			_a9781603272230
024	7		_a10.1007/978-1-60327-223-0 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC
245	1	0	_aProtein Folding, Misfolding, and Disease _bMethods and Protocols _cedited by Andrew F. Hill, Kevin J. Barnham, Stephen P. Bottomley, Roberto Cappai.
250			_a1st edition 2011
264		1	_aTotowa, NJ _bHumana Press _c2011
300			_a1 recurso en línea (X, 230 páginas) _b50 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 _v752
505	0		_aStrategies for Boosting the Accumulation of Correctly Folded Recombinant Proteins Expressed in Escherichia coli -- An Escherichia coli Cell-Free System for Recombinant Protein Synthesis on a Milligram Scale -- Synthesis of Peptide Sequences Derived from Fibril-Forming Proteins -- Refolding Your Protein with a Little Help from REFOLD -- Circular Dichroism and Its Use in Protein Folding Studies -- Distance Measurements by Continuous Wave EPR Spectroscopy to Monitor Protein Folding -- Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding -- Diagnostics for Amyloid Fibril Formation: Where to Begin -- Probing Protein Aggregation with Quartz Crystal Microbalances -- Dried and Hydrated X-Ray Scattering Analysis of Amyloid Fibrils -- Solid-State NMR of Amyloid Membrane Interactions -- Sedimentation Velocity Analysis of Amyloid Fibrils -- Transmission Electron Microscopy of Amyloid Fibrils -- Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin -- Elucidating the Role of Metals in Alzheimer's Disease through the Use of Surface Enhanced Laser Desorption / Ionisation Time-of-Flight Mass Spectrometry.
520			_aProtein misfolding is a key feature of many disorders in humans, given that over twenty proteins are known to misfold and cause disease.  In Protein Folding, Misfolding, and Disease: Methods and Protocols, experts in the field present a collection of current methods for studying the analysis of protein folding and misfolding, featuring strategies for expressing and refolding recombinant proteins which can then be utilized in subsequent experiments. This detailed volume also covers methods for analyzing the formation of amyloid, protocols for determining the size and structure of native and misfolded proteins, as well as specific examples of where misfolded proteins can be examined using state-of -the-art technologies. Written in the highly successful Methods in Molecular Biology™ series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.   Up to date and authoritative, Protein Folding, Misfolding, and Disease: Methods and Protocols offers researchers the tools necessary to move ahead in this vital field.
700	1		_aHill, Andrew F _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
700	1		_aBarnham, Kevin J _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
700	1		_aBottomley, Stephen P _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
700	1		_aCappai, Roberto _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
776	0	8	_iPrinted edition: _z9781603272216
776	0	8	_iPrinted edition: _z9781617791680
776	0	8	_iPrinted edition: _z9781493956890
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-60327-223-0 _z(usuarios Universidad Europea de Valencia)
942			_2lcc _cLE
988			_aSpringer_Protocols_2011
999			_c235214 _d235214