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Intrinsically Disordered Proteins

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Chapman & Hall/CRC
Physics, Science / Physics, Sc
The Physical Object
FormatHardcover
ID Numbers
Open LibraryOL11817485M
ISBN 101420078925
ISBN 139781420078923

Intrinsically Disordered Proteins: Dynamics, Binding, and Function thoroughly examines and ties together the fundamental biochemical functions of IDPs and IDRs, including signaling, binding, and regulation, with methodology for study and associated pathways for drug design and therapeutic intervention.

The role of new mechanistic, computational, and experimental Format: Paperback. 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 book focuses on physical techniques for the identification and characterization of by: : Intrinsically Disordered Proteins Studied by NMR Spectroscopy (Advances in Experimental Medicine and Biology) (): Isabella C.

Felli, Roberta Pierattelli: Books. Intrinsically Disordered Proteins, Volumethe 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 Intrinsically Disordered Proteins book.

About this book 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.

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. 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. About this book 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. Intrinsically disordered proteins (IDPs) are a class of proteins that are rapidly turning upside down the dogmatic idea that structure encodes function in proteins 1, Proteins that were previously ignored because they Intrinsically Disordered Proteins book large structurally disordered regions are now emerging as important contributors to a myriad of functions ranging from regulation of stress response to Author: Stefan Roberts.

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.

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 book focuses on physical techniques for the identification and characterization of IDPs.

About this book Instrumental techniques for analyzing intrinsically disordered proteins "With contributions from an international selection of leading researchers, this book fills an important need in a rapidly growing field.

About this book 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).Brand: Springer International Publishing.

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. 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. 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).Cited by: These intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) exist as structural ensembles either at the secondary or at the tertiary structure level.

This chapter presents the currently available strategies for effective inhibition of disorder‐based protein by: Receive an update when the latest chapters in this book series are published.

Sign in to set up alerts Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins. Spectroscopic Characterization of Structure–Function Relationships in the Intrinsically Disordered Protein. Phase separation of intrinsically disordered proteins / Ammon E.

Posey, Alex S. Holehouse, and Rohit V. Pappu --Methods and strategies to quantify phase separation of disordered proteins / Alfredo Vidal Ceballos, Charles J. McDonald, and Shana Elbaum-Garfinkle --Visualization and quantitation of phase-separated droplet formation by human HP1.

Open Library is an open, editable library catalog, building towards a web page for every book ever published. Intrinsically Disordered Proteins by Vladimir N. Uversky,Springer edition, paperback.

Abstract Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid by: (A) Amino acid determinants defining structural and functional differences between the ordered and intrinsically disordered proteins.

Fractional difference in the amino acid composition (compositional profile) between the typical IDPs from the DisProt database [ 47] and a set of completely ordered proteins [ 48] Cited by: 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. Intrinsically disordered proteins (IDPs) in cells phase separate to form diverse membraneless organelles, which have condensed liquid droplet-like properties and often contain multiple IDPs.

However, how potential interactions between different IDPs affect the dynamic behavior of these protein droplets is laAuthor: Yongsang Jo, Yongwon Jung.

Studies of these intrinsically disordered proteins (IDPs) are in the spotlight of current structural biology, leading to a rapid extension and transformation of the structure–function paradigm.

Predictions based on the biased sequence features of IDPs suggest that structural disorder reaches very high proportions in higher by: 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-functio. An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure.

[2] [3] [4] IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers.

They constitute one of the main types of protein (alongside. Importantly, transcriptome-wide analysis of mRNAs that encode intrinsically disordered proteins revealed that each has structured regions that could be targeted with small molecules.

These findings demonstrate the potential for targeting undruggable proteins at the level of their coding : Zhang P, Park Hj, Zhang J, Junn E, Andrews Rj, Velagapudi Sp, Abegg D, Vishnu K, Costales Mg, Childs.

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David J. Scott, Donald J. Winzor, in Methods in Enzymology, 4 Concluding Remarks. Intrinsically disordered proteins are of immense interest due to both their diverse biological roles and also their apparent abrogation of the structure-equals-function paradigm. As such many diverse biophysical techniques can be applied to their analysis in the view that a new.

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).

Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A. Edited by Vladimir N.

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Uversky. Intrinsically disordered proteins in the formation of functional amyloids from bacteria to humans.

Book chapter Full text access Chapter Ten - The dark proteome of cancer: Intrinsic disorderedness and functionality of.DisProt is a database of intrinsically disordered proteins.

Disordered regions are manually curated from literature.

Description Intrinsically Disordered Proteins FB2

DisProt annotations cover both structural and functional aspects of disorder detected by specific experimental methods. Annotation concepts and detection methods are encoded in the Disorder Ontology.

Read more about DisProt. While the majority of proteins fold into well-defined structures to function, a substantial fraction of the proteome is made up by intrinsically disordered proteins (IDPs) (Uversky and Dunker, ).These IDPs, which can be fully disordered or contain disordered regions of variable size, play pivotal roles in biology, usually by participating in protein-protein Cited by: