國立虎尾科技大學 |

Intrinsically Disordered Proteins Studied by NMR Spectroscopy

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Intrinsically Disordered Proteins Studied by NMR Spectroscopy/ edited by Isabella C. Felli, Roberta Pierattelli.
other author:	Felli, Isabella C.
Description:	XIII, 421 p. 111 illus., 98 illus. in color.online resource. :
Contained By:	Springer Nature eBook
Subject:	Bioinformatics. -
Online resource:	https://doi.org/10.1007/978-3-319-20164-1
ISBN:	9783319201641

Intrinsically Disordered Proteins Studied by NMR Spectroscopy
Intrinsically Disordered Proteins Studied by NMR Spectroscopy[electronic resource] /edited by Isabella C. Felli, Roberta Pierattelli. - 1st ed. 2015. - XIII, 421 p. 111 illus., 98 illus. in color.online resource. - Advances in Experimental Medicine and Biology,8700065-2598 ;. - Advances in Experimental Medicine and Biology,889.

Nuclear 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 Men” Situation -- 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.

This 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.

ISBN: 9783319201641

Standard No.: 10.1007/978-3-319-20164-1doiSubjects--Topical Terms:

583857
Bioinformatics.

LC Class. No.: QH324.2-324.25

Dewey Class. No.: 570.285

Intrinsically Disordered Proteins Studied by NMR Spectroscopy
LDR:03945nam a22004215i 4500 001 961349
003 DE-He213
005 20200630180549.0
007 cr nn 008mamaa
008 201211s2015 gw | s |||| 0|eng d
020 $a 9783319201641 $9 978-3-319-20164-1
024 7 $a 10.1007/978-3-319-20164-1 $2 doi
035 $a 978-3-319-20164-1
050 4 $a QH324.2-324.25
072 7 $a PSD $2 bicssc
072 7 $a SCI056000 $2 bisacsh
072 7 $a PSD $2 thema
072 7 $a UB $2 thema
082 0 4 $a 570.285 $2 23
245 1 0 $a Intrinsically Disordered Proteins Studied by NMR Spectroscopy $h [electronic resource] / $c edited by Isabella C. Felli, Roberta Pierattelli.
250 $a 1st ed. 2015.
264 1 $a Cham : $b Springer International Publishing : $b Imprint: Springer, $c 2015.
300 $a XIII, 421 p. 111 illus., 98 illus. in color. $b online resource.
336 $a text $b txt $2 rdacontent
337 $a computer $b c $2 rdamedia
338 $a online resource $b cr $2 rdacarrier
347 $a text file $b PDF $2 rda
490 1 $a Advances in Experimental Medicine and Biology, $x 0065-2598 ; $v 870
505 0 $a Nuclear 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 Men” Situation -- 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 $a This 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.
650 0 $a Bioinformatics. $3 583857
650 0 $a Proteins . $3 1253493
650 0 $a Cell biology. $3 1253486
650 2 4 $a Protein Science. $3 782127
650 2 4 $a Cell Biology. $3 593889
700 1 $a Felli, Isabella C. $4 edt $4 http://id.loc.gov/vocabulary/relators/edt $3 1068870
700 1 $a Pierattelli, Roberta. $4 edt $4 http://id.loc.gov/vocabulary/relators/edt $3 1068871
710 2 $a SpringerLink (Online service) $3 593884
773 0 $t Springer Nature eBook
776 0 8 $i Printed edition: $z 9783319201634
776 0 8 $i Printed edition: $z 9783319201658
776 0 8 $i Printed edition: $z 9783319371177
830 0 $a Advances in Experimental Medicine and Biology, $x 0065-2598 ; $v 889 $3 1253792
856 4 0 $u https://doi.org/10.1007/978-3-319-20164-1
912 $a ZDB-2-SBL
912 $a ZDB-2-SXB
950 $a Biomedical and Life Sciences (SpringerNature-11642)
950 $a Biomedical and Life Sciences (R0) (SpringerNature-43708)