The Three Functional States of Proteins: Structured, Intrinsically Disordered, and Phase Separated - Brossura

Brossura

ISBN 10: 0443218099 ISBN 13: 9780443218095

Casa editrice: Academic Pr, 2024

Riassunto

The Three Functional States of Proteins explores how structured proteins, intrinsically disordered proteins, and phase separated proteins contribute to the complexity of cellular life, and offers insights into their roles in both health and disease. It discusses the latest research findings and highlight groundbreaking discoveries and innovative methodologies used to study these protein states.
Traditionally, the different states of proteins have been defined based on their structures and functions. However, it is becoming increasingly clear that these criteria alone may not be sufficient to capture the complex and multifaceted properties of these molecules. Definitions based on thermodynamics and kinetics are now recognized as potentially more appropriate for comprehensively understanding protein states. Emerging evidence indicates that under physiological conditions, a majority of proteins possess the capability to exist in and transition between the native, droplet, and amyloid states. These distinct states play crucial roles in various cellular functions, influenced significantly by their physicochemical and structural properties. The book also considers the interactions among these states and discusses how their internal organization as individual molecules, as well as their collective organization as molecular assemblies are stabilized. Furthermore, it examines the processes by which these states are formed and the cellular functions associated with each specific state.

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Informazioni sugli autori

Professor Timir Tripathi is a Professor of Molecular Biology, School of Life Sciences, North-Eastern Hill University, Shillong, India. Earlier, he served as the Regional Director of Indira Gandhi National Open University. His previous role was Senior Assistant Professor and Principal Investigator at the Department of Biochemistry, NEHU, Shillong. He holds a Ph.D. from Jawaharlal Nehru University, New Delhi. His primary research focus is studying the conformational dynamics, interaction, and stabilization of the complexes formed by intrinsically disordered neuropathological protein aggregates, their properties of liquid-liquid phase separation, interaction, and roles in nucleocytoplasmic transport in neurodegenerative diseases. Professor Tripathi is an Associate Fellow of the Indian National Science Academy, New Delhi, and an elected member of the National Academy of Sciences, India, the Royal Society of Chemistry, and the Royal Society of Biology, UK

Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his PhD from Moscow Institute of Physics and Technology and D.Sc. from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. Since 2010, Professor Uversky has worked at University of South Florida, where he works on various aspects of protein intrinsic disorder phenomenon and analysis of protein folding and misfolding processes. He has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He also servs as an editor in a number of scientific journals.

Dalla quarta di copertina

Traditionally, different states of proteins have been defined based on their structures and functions. However, it is becoming increasingly clear that these criteria may not be sufficient to capture the complex properties of these molecules and that definitions based on thermodynamics and kinetics could be more appropriate. Emerging evidence indicates that under physiological conditions, most proteins can sample the native, droplet, and amyloid states. These states contribute to different cellular functions in accordance with their physical and structural properties.

The native monomeric or oligomeric state of a protein is typically the most frequently observed state under cellular conditions. The biological functions of proteins are associated with this native state. Proteins in this functional state can be highly structured or intrinsically disordered (i.e., exist as highly dynamic structural ensembles of interconverting conformations), or they can combine features of order and disorder.

The amyloid state with its cross-β structure is a solid-like condensed state that is thermodynamically stable at the cellular concentrations of proteins, and therefore its formation tends to be irreversible. Although many known examples of amyloids are related to the pathogenesis of various human diseases, functional amyloids are found in all kingdoms of life.

The droplet or phase-separated state is a liquid-like condensed state formed by the non-stoichiometric assembly of protein molecules, often via interaction with nucleic acids. This is the functional state of many membrane-less organelles, which are now considered major organizing elements of intracellular space.

This book provides comprehensive coverage of these three protein states and their thermodynamics and kinetic properties. The book also considers their interactions and discuss how their internal organization as individual molecules and their collective organization as molecular assemblies are stabilized. It also discusses how these states are formed and examines the cellular functions associated with the specific states.

Dettagli dell?edizione

• Editore: Academic Pr
• Data di pubblicazione: 2024
• Lingua: Inglese
• ISBN 10: 0443218099
• ISBN 13: 9780443218095
• Rilegatura: Copertina flessibile
• Numero edizione: 1
• Numero di pagine: 450
• Redattore: Tripathi Timir, Uversky Vladimir N.
• Contatto del produttore: Academic Press; https://shop.elsevier.com/; ; 230 PARK AVENUE, SUITE 800; NY; NY; 10169; U.S.A.
• Persona responsabile: non disponibile