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Intrinsically disordered proteins st...

Felli, Isabella C.

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Intrinsically disordered proteins studied by NMR spectroscopy

Record Type:	Electronic resources : Monograph/item
Title/Author:	Intrinsically disordered proteins studied by NMR spectroscopy/ edited by Isabella C. Felli, Roberta Pierattelli.
other author:	Felli, Isabella C.
Published:	Cham :Springer International Publishing : : 2015.,
Description:	xiii, 421 p. :ill. (some col.), digital ;24 cm.
[NT 15003449]:	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.
Contained By:	Springer eBooks
Subject:	Proteins - Spectra. -
Online resource:	http://dx.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. - Cham :Springer International Publishing :2015. - xiii, 421 p. :ill. (some col.), digital ;24 cm. - Advances in experimental medicine and biology,v.8700065-2598 ;. - Advances in experimental medicine and biology ;946..

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:

687705
Proteins
--Spectra.

LC Class. No.: QP551

Dewey Class. No.: 572.6

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245 0 0 $a Intrinsically disordered proteins studied by NMR spectroscopy $h [electronic resource] / $c edited by Isabella C. Felli, Roberta Pierattelli.
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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 Proteins $x Spectra. $3 687705
650 0 $a Nuclear magnetic resonance spectroscopy. $3 560451
650 1 4 $a Life Sciences. $3 890838
650 2 4 $a Bioinformatics. $3 553671
650 2 4 $a Protein Science. $3 1067276
650 2 4 $a Cell Biology. $3 892383
700 1 $a Felli, Isabella C. $3 2162130
700 1 $a Pierattelli, Roberta. $3 2162131
710 2 $a SpringerLink (Online service) $3 836513
773 0 $t Springer eBooks
830 0 $a Advances in experimental medicine and biology ; $v 946. $3 1565434
856 4 0 $u http://dx.doi.org/10.1007/978-3-319-20164-1
950 $a Biomedical and Life Sciences (Springer-11642)