000			04153nam a22003975i 4500
001			81462
003			ES-MaUEC
005			20230207040331.0
007			cr nn 008mamaa
008			150919s2015 gw | s |||| 0|eng d
020			_a9783319201641
024	7		_a10.1007/978-3-319-20164-1 _2doi
050		4	_aQP551 _b.I587 2015
245	1	0	_aIntrinsically Disordered Proteins Studied by NMR Spectroscopy _cedited by Isabella C. Felli, Roberta Pierattelli.
250			_a1st ed. 2015.
260			_aCham, Switzerland _bSpringer _c2015
300			_a1 recurso en línea (XIII, 421 páginas) _b111 ilustraciones, 98 ilustraciones en color
336			_aTexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aAdvances in Experimental Medicine and Biology _x0065-2598 _v870
505	0		_aNuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins -- Structure and Dynamics of Intrinsically Disordered Proteins -- NMR methods for the study of IDP structure, dynamics and interactions: general overview and practical guidelines -- Ensemble Calculation for IDPs Using NMR Parameters -- NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins -- Recombinant IDPs for NMR: Tips and Tricks -- Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an “Elephant and Blind Menâ€{u04E9}tuation -- Application of SAXS for the Structural Characterization of IDPs -- Bioinformatics Approaches for Predicting Disordered Protein Motifs -- Towards Understanding Protein Disorder In-Cell -- The Protein Ensemble Database -- Order and Disorder in the Replicative Complex of Paramyxoviruses -- Druggability of Intrinsically Disordered Proteins -- Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer's Disease.
520	3		_aThis book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). The properties of IDPs and IDPRs are highly complementary to those deriving from the presence of a unique and well-defined three-dimensional fold. Ignored for a long time in high-resolution studies of proteins, intrinsic protein disorder is now recognized as one of the key features for a large variety of cellular functions, where structural flexibility presents a functional advantage in terms of binding plasticity and promiscuity and this volume explores this exciting new research. Recent progress in the field has radically changed our perspective to study IDPs through NMR: increasingly complex IDPs can now be characterized, a wide range of observables can be determined reporting on the structural and dynamic properties, computational methods to describe the structure and dynamics are in continuous development and IDPs can be studied in environments as complex as whole cells. This volume communicates the new exciting possibilities offered by NMR and presents open questions to foster further developments. Intrinsically Disordered Proteins Studied by NMR Spectroscopy provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.
710	2		_aSpringerLink (Online service) _0Local _9106996
942			_2lcc _cLE
988			_aEBOOK, EBSPRINGER, asignarmaterias_11febrero
650		7	_aProteínas _2embne _9139861
650		7	_aCitología _2embne _9139477
650	2	7	_aProteínas _2embne _9139861
700	1		_aFelli, Isabella C. _eeditor literario _0Local _993904
700	1		_aPierattelli, Roberta _eeditor literario _993905 _0Local
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-319-20164-1 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12900527 _b10-10-17 _c18-01-16
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _ggw _h0
945			_aQP551 .I587 2015 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11570143 _z06-04-17
999			_c81462 _d81462 _x1