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008			100301s1995 xxu| o |||| 0|eng d
020			_a9781592595273
024	7		_a10.1385/0896033015 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP551 _b1995 EB
100	1		_aShirley, Bret A. _eautor _9689041
245	1	0	_aProtein Stability and Folding : _bTheory and Practice _cby Bret A. Shirley
250			_a1st edition 1995
264		1	_aTotowa, NJ _bHumana Press _c1995
300			_a1 recurso en línea (X, 377 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 _v40
505	0		_aNoncovalent Forces Important to the Conformational Stability of Protein Structures -- Degradative Covalent Reactions Important to Protein Stability -- Fluorescence Spectroscopy -- Ultraviolet Absorption Spectroscopy -- Circular Dichroism -- Infrared Spectroscopy -- Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping -- Urea and Guanidine Hydrochloride Denaturation Curves -- Differential Scanning Calorimetry -- Disulfide Bonds in Protein Folding and Stability -- Solvent Stabilization of Protein Structure -- Site-Directed Mutagenesis to Study Protein Folding and Stability -- Hydrogen Exchange Techniques -- Protein Folding Kinetics -- Molten Globules -- Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES.
520			_aThe intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The development of recombinant DNA techniques has made possible the production of large quantities of virtually any protein, as well as the production of proteins with altered amino acid sequence. Improvements in instrumentation, and the development and refinement of new techniques for studying these recombinant proteins, has been central to the progress made in this field. To give the reader adequate background information about the s- ject, the first two chapters of this book review two different, yet related, aspects of protein stability. The first chapter presents a review of our current understanding of the forces involved in determining the conf- mational stability of proteins as well as their three-dimensional folds. The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Although some techniques, such as X-ray crystallography and mass spectroscopy, are used in the study of protein stability, they are beyond the scope of this book and will not be covered extensively.
988			_aSpringer_Protocols_1995
650		7	_2embne _9139861 _aProteínas
776	0	8	_iPrinted edition: _z9781489940667
776	0	8	_iPrinted edition: _z9780896033016
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/0896033015 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b10/2023 _dz _eb _zSI