Intrinsically Disordered Proteins

Intrinsically Disordered Proteins: Dynamics, Binding, and Function thoroughly examines and ties together the fundamental biochemical functions of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs), including signaling, binding, and regulation, with the methodology for study and the associated pathways for drug design and therapeutic intervention. The role of new mechanistic, computational, and experimental approaches in IDP study are explored in depth, with methods for the characterization of IDP dynamics; models, simulations, and mechanisms of IDP and IDR binding; and biological and medical implications of IDP dynamics prominently featured. Written and edited by leading scientists in the field, this book explores groundbreaking areas such as ensemble descriptions of IDPs and IDRs, single-molecule studies of IDPs and IDRs, IDPs and IDRs in membraneless organelles, and molecular mechanisms of fibrillation of IDPs. Intrinsically Disordered Proteins provides students and researchers in biochemistry, molecular biology, and applied microbiology with a comprehensive and updated discussion of the complex dynamics of IDPs and IDRs. Provides in-depth discussion of fundamental IDP and IDR dynamics, function, and binding, with mechanistic insight to support new drug development Describes the role of new computational and experimental approaches in characterizing the binding of IDPs to their functional targets Features chapter contributions from international experts in IDP and IDR biochemical function and methods of study

Produk Detail:

  • Author : Nicola Salvi
  • Publisher : Academic Press
  • Pages : 355 pages
  • ISBN : 0128167327
  • Rating : 4/5 from 21 reviews
CLICK HERE TO GET THIS BOOKIntrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins
  • Author : Nicola Salvi
  • Publisher : Academic Press
  • Release : 14 June 2019
GET THIS BOOKIntrinsically Disordered Proteins

Intrinsically Disordered Proteins: Dynamics, Binding, and Function thoroughly examines and ties together the fundamental biochemical functions of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs), including signaling, binding, and regulation, with the methodology for study and the associated pathways for drug design and therapeutic intervention. The role of new mechanistic, computational, and experimental approaches in IDP study are explored in depth, with methods for the characterization of IDP dynamics; models, simulations, and mechanisms of IDP and IDR binding; and

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins
  • Author : Nicola Salvi
  • Publisher : Academic Press
  • Release : 15 September 2019
GET THIS BOOKIntrinsically Disordered Proteins

A growing body of evidence highlights the importance of intrinsically disordered proteins (IDPs) and regions (IDRs) in fundamental cellular functions and biochemical processes. Increasing evidence associates alterations in the expression levels or activity of IDPs with human pathologies; and, in recent years, researchers have placed stronger emphasis on developing computational and experimental approaches to describe binding of IDPs to their functional targets, and establish drug designs for new therapeutics acting on IDPs and IDRs. Intrinsically Disordered Proteins: Dynamics, Binding, and

Structure and Function of Intrinsically Disordered Proteins

Structure and Function of Intrinsically Disordered Proteins
  • Author : Peter Tompa,Alan Fersht
  • Publisher : CRC Press
  • Release : 18 November 2009
GET THIS BOOKStructure and Function of Intrinsically Disordered Proteins

The existence and functioning of intrinsically disordered proteins (IDPs) challenge the classical structure-function paradigm that equates function with a well-defined 3D structure. Uncovering the disordered complement of proteomes and understanding their functioning can extend the structure-function paradigm to herald new breakthroughs in drug development. Structure and Function of Intrinsically Disordered Proteins thoroughly covers the history up to the latest developments in this field. After examining the principles of protein structure, the classical paradigm, and the history of structural disorder, the

Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology

Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology
  • Author : Vladimir Uversky
  • Publisher : Academic Press
  • Release : 15 September 2019
GET THIS BOOKDancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology

"Dancing protein clouds: Intrinsically disordered proteins in the norm and pathology" represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins. Topics in this update include structural and functional characterization of several important intrinsically disordered proteins, such as 14-3-3 proteins and their partners, as well as proteins from muscle sarcomere; representation of intrinsic disorder-related concept of protein structure-function continuum; discussion of the role of intrinsic disorder in phenotypic switching; consideration of the

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins
  • Author : Vladimir N. Uversky
  • Publisher : Springer
  • Release : 05 August 2014
GET THIS BOOKIntrinsically Disordered Proteins

In this brief, Vladimir Uversky discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). Beginning with an introduction to the concept of protein intrinsic disorder, Uversky then goes on to describe the peculiar amino acid sequences of IDPs, their structural heterogeneity, typical functions and disorder-based binding modes. In the final sections, Uversky discusses IDPs in human diseases and as potential drug targets. This volume provides a snapshot to researchers

Intrinsically Disordered Proteins Studied by NMR Spectroscopy

Intrinsically Disordered Proteins Studied by NMR Spectroscopy
  • Author : Isabella C. Felli,Roberta Pierattelli
  • Publisher : Springer
  • Release : 19 September 2015
GET THIS BOOKIntrinsically Disordered Proteins Studied by NMR Spectroscopy

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

Instrumental Analysis of Intrinsically Disordered Proteins

Instrumental Analysis of Intrinsically Disordered Proteins
  • Author : Vladimir Uversky,Sonia Longhi
  • Publisher : John Wiley & Sons
  • Release : 31 January 2011
GET THIS BOOKInstrumental Analysis of Intrinsically Disordered Proteins

Instrumental techniques for analyzing intrinsically disordered proteins The recently recognized phenomenon of protein intrinsic disorder is gaining significant interest among researchers, especially as the number of proteins and protein domains that have been shown to be intrinsically disordered rapidly grows. The first reference to tackle this little-documented area, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation provides researchers with a much-needed, comprehensive summary of recent achievements in the methods for structural characterization of intrinsically disordered proteins (IDPs). Chapters

Intrinsically Disordered Proteins (IDPs)

Intrinsically Disordered Proteins (IDPs)
  • Author : Violet Weber
  • Publisher : Unknown Publisher
  • Release : 17 April 2021
GET THIS BOOKIntrinsically Disordered Proteins (IDPs)

Intrinsically disordered proteins (IDPs) are biomolecules that do not have a definite 3D structure; their role in the biochemical network of a cell relates to their ability to switch rapidly among different secondary and tertiary structures. The emergence of IDPs has challenged the classical protein structure-function paradigm. IDPs play an important role in cellular regulation, signaling and control in health and disease. However, the unusual biophysics of these proteins makes structural characterization of IDPs and their complexes not only challenging

Intrinsically Disordered Protein Analysis

Intrinsically Disordered Protein Analysis
  • Author : Vladimir N. Uversky,A. Keith Dunker
  • Publisher : Humana Press
  • Release : 05 July 2012
GET THIS BOOKIntrinsically Disordered Protein Analysis

Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins. Structural biologists now recognize that the functional diversity provided by disordered regions complements the functional repertoire of ordered protein regions. In Intrinsically Disordered Protein Analysis :Methods and Experimental Tools, expert researchers explore the high abundance of IDPs in various organisms, their unique structural features, numerous functions, and crucial associations with different diseases. Volume 1 includes sections on

Intrinsically Disordered Protein Analysis

Intrinsically Disordered Protein Analysis
  • Author : Vladimir N. Uversky,A. Keith Dunker
  • Publisher : Humana Press
  • Release : 05 July 2012
GET THIS BOOKIntrinsically Disordered Protein Analysis

Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins. Structural biologists now recognize that the functional diversity provided by disordered regions complements the functional repertoire of ordered protein regions. In Intrinsically Disordered Protein Analysis :Methods and Experimental Tools, expert researchers explore the high abundance of IDPs in various organisms, their unique structural features, numerous functions, and crucial associations with different diseases. Volume 1 includes sections on

Structural Biology in Drug Discovery

Structural Biology in Drug Discovery
  • Author : Jean-Paul Renaud
  • Publisher : John Wiley & Sons
  • Release : 09 January 2020
GET THIS BOOKStructural Biology in Drug Discovery

With the most comprehensive and up-to-date overview of structure-based drug discovery covering both experimental and computational approaches, Structural Biology in Drug Discovery: Methods, Techniques, and Practices describes principles, methods, applications, and emerging paradigms of structural biology as a tool for more efficient drug development. Coverage includes successful examples, academic and industry insights, novel concepts, and advances in a rapidly evolving field. The combined chapters, by authors writing from the frontlines of structural biology and drug discovery, give readers a valuable

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins
  • Author : Anonim
  • Publisher : Academic Press
  • Release : 21 November 2018
GET THIS BOOKIntrinsically Disordered Proteins

Intrinsically Disordered Proteins, Volume 611, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics of interest, including the Characterization of Structure-Function relationships in the intrinsically disordered protein complexin, Distances, distance distributions, and ensembles of IDPs from single-molecule FRET, Biophysical characterization of disordered protein liquid phases, The Use of Mass Spectrometry to Examine IDPs – Unique Insights and Caveats, Fluorescence Depolarization Kinetics to Study Conformational Preference, Structural Plasticity

Measles Virus Nucleoprotein

Measles Virus Nucleoprotein
  • Author : Sonia Longhi
  • Publisher : Nova Publishers
  • Release : 17 April 2021
GET THIS BOOKMeasles Virus Nucleoprotein

Measles virus possesses a non segmented, single stranded, negative sense RNA genome that is encapsidated by the nucleoprotein to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein. This book focuses on the main structural information available on the nucleoprotein, showing that it consists of a structured core (NCORE) and of an intrinsically disordered C-terminal domain (NTAIL). The functional implications

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins
  • Author : Birthe B Kragelund,Karen Skriver
  • Publisher : Humana
  • Release : 05 July 2020
GET THIS BOOKIntrinsically Disordered Proteins

The edition details methods to study intrinsically disordered proteins (IDPs) including recent topics such as extremely high-affinity disordered complexes, kinetics that evade established concepts, liquid-liquid phase separation, and novel disorder-driven allosteric mechanisms. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Intrinsically Disordered Proteins: Methods and Protocols aims

Fuzziness

Fuzziness
  • Author : Monika Fuxreiter,Peter Tompa
  • Publisher : Springer Science & Business Media
  • Release : 07 March 2012
GET THIS BOOKFuzziness

Detailed characterization of fuzzy interactions will be of central importance for understanding the diverse biological functions of intrinsically disordered proteins in complex eukaryotic signaling networks. In this volume, Peter Tompa and Monika Fuxreiter have assembled a series of papers that address the issue of fuzziness in molecular interactions. These papers provide a broad overview of the phenomenon of fuzziness and provide compelling examples of the central role played by fuzzy interactions in regulation of cellular signaling processes and in viral