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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 entering the field as well as providing a current overview for more experienced scientists in related areas.
Proteins --- Structure. --- Conformation. --- Protein conformation --- Biochemistry. --- Protein Structure. --- Medicinal Chemistry. --- Biochemistry, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Composition --- Proteins . --- Medicinal chemistry. --- Chemistry, Medical and pharmaceutical --- Chemistry, Pharmaceutical --- Drug chemistry --- Drugs --- Medical chemistry --- Medicinal chemistry --- Pharmacochemistry --- Proteids --- Biomolecules --- Polypeptides --- Proteomics
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Droplets of Life: Membrane-Less Organelles, Biomolecular Condensates, and Biological Liquid–Liquid Phase Separation provides foundational information on the biophysics, biogenesis, structure, functions, and roles of membrane-less organelles. The study of liquid–liquid phase separation has attracted a lot of attention from disciplines such as cell biology, biophysics, biochemistry, and others trying to understand how, why, and what roles these condensates play in homeostasis and disease states in living organisms. This book's editor recruited a group of international experts to provide a current and authoritative overview of all aspects associated with this exciting area. Sections introduce membrane-less organelles (MLOs) and biomolecular condensates; MLOs in different sizes, shapes, and composition; and the formation of MLOs due to phase separation and how it can tune reactions, organize the intracellular environment, and provide a role in cellular fitness.
Cell organelles. --- Organelles, Cell --- Cytoplasm --- Biomolecular Condensates --- Organelles --- Phase Separation --- Biomolecular Condensates. --- Organelles. --- Phase Separation.
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This book is an embodiment of a series of articles that were published as part of a Special Issue of Biomolecules. It is dedicated to exploring the role of intrinsically disordered proteins (IDPs) in various chronic diseases. The main goal of the articles is to describe recent progress in elucidating the mechanisms by which IDPs cause various human diseases, such as cancer, cardiovascular disease, amyloidosis, neurodegenerative diseases, diabetes, and genetic diseases, to name a few. Contributed by leading investigators in the field, this compendium serves as a valuable resource for researchers, clinicians as well as postdoctoral fellows and graduate students
IDP --- fuzzy interactions --- protein complementation assays --- split-GFP reassembly --- kinetics --- membraneless organelles --- optical tweezer --- liquid–liquid phase separation --- protein diffusion --- depletion interaction --- entropic force --- low-complexity sequences --- intrinsically disordered proteins --- PAGE4 --- conformational plasticity --- order–disorder transition --- phosphorylation --- intrinsic disordered protein --- extremely fuzzy complex --- protein interaction --- binding mechanism --- tumor protein p53 --- mouse double minute 2 --- mouse double minute 4 --- Kinase-inducible domain interacting domain --- phosphomimetics --- nuclear magnetic resonance --- transient secondary structure --- COR15A --- Late embryogenesis abundant --- Trifluoroethanol --- Nuclear magnetic resonance --- intrinsically disordered regions --- functional segments --- disease-related proteins --- protein-protein interaction --- subcellular location --- glucocorticoid receptor --- intrinsically disordered --- transactivation activity --- gene regulation --- coactivators --- microtubule associated protein --- tau --- intrinsically disordered protein --- dynamic configuration --- free energy landscape --- microtubules --- electrostatics --- diffusion --- protein structure prediction --- molecular modelling --- molecular dynamics --- tau–microtubule association --- conformational ensemble --- replica exchange molecular dynamics --- drug design --- n/a --- liquid-liquid phase separation --- order-disorder transition --- tau-microtubule association
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Protein Misfolding, Aggregation, and Conformational Disease, is the first book to discuss significant achievements in protein structure-function relationships in the areas of biochemistry, molecular biology and molecular medicine. This volume summarizes recent achievements in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders. Research indicates that various human disorders, including most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. Protein Misfolding, Aggregation and Conformational Diseases is an ideal book for biochemists, protein scientists, immunologists, pharmaceutical scientists, and molecular and cellular biologists.
Protein folding. --- Proteins --- Conformation. --- Protein conformation --- Folding of proteins --- Folding --- Conformation --- Life sciences. --- Immunology. --- Cytology. --- Life Sciences, general. --- Cell Biology. --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Immunobiology --- Life sciences --- Serology --- Biosciences --- Sciences, Life --- Science --- Cell biology.
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Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and ins
Biomedical engineering. --- Nanotechnology. --- Molecular technology --- Nanoscale technology --- High technology --- Clinical engineering --- Medical engineering --- Bioengineering --- Biophysics --- Engineering --- Medicine --- Protein folding --- Imaging systems. --- Computer simulation.
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Protein Misfolding, Aggregation and Conformational Diseases, Part B: Molecular Mechanisms of Conformational Diseases, is a comprehensive volume providing a broad and detailed discussion of the relationships of protein misfolding and aggregation with the pathogenesis of numerous conformational diseases. While the Part A was dedicated to the description of the general mechanisms underlying protein misfolding, aggregation, and development of protein deposition disorders, this volume summarizes recent achievements in the understanding of the molecular mechanisms of conformational diseases. Research indicates that these mechanisms are highly diverse and range from the altered protein structure leading to the enhanced propensity for aggregation/deposition or the impaired functions and ending with changes in supra-molecular structures or posttranslational modification. Protein Misfolding, Aggregation and Conformational Diseases, Part B: Molecular Mechanisms of Conformational Diseases, is an ideal book for pharmaceutical scientists, molecular and cellular biologists, biochemists, immunologists, protein scientists, and biophysicists.
Protein folding. --- Cell aggregation. --- Proteins --- Pathophysiology. --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Aggregation, Cell --- Cell patterning --- Cell interaction --- Microbial aggregation --- Folding of proteins --- Folding --- Conformation --- Immunology. --- Cytology. --- Cell Biology. --- Immunobiology --- Life sciences --- Serology --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Cell biology.
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Structure and Intrinsic Disorder in Enzymology offers a direct, yet comprehensive presentation of the fundamental concepts, characteristics and functions of intrinsically disordered enzymes, along with valuable notes and technical insights powering new research in this emerging field. Here, more than twenty international experts examine protein flexibility and cryo-enzymology, hierarchies of intrinsic disorder, methods for measurement of disorder in proteins, bioinformatics tools for predictions of structure, disorder and function, protein promiscuity, protein moonlighting, globular enzymes, intrinsic disorder and allosteric regulation, protein crowding, intrinsic disorder in post-translational, and much more. Chapters also review methods for study, as well as evolving technology to support new research across academic, industrial and pharmaceutical labs.
Enzymes.. --- Enzymes --- Structure. --- Biocatalysts --- Ferments --- Soluble ferments --- Catalysts --- Proteins --- Enzymology --- Intrinsically Disordered Proteins --- Intrinsically Disordered Proteins. --- Enzymes.
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In biochemistry, a metalloprotein is a generic term for a protein that contains a metal cofactor. The metal may be an isolated ion or may be coordinated with a nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clusters Metalloproteins deals with all aspects related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The biological roles of metal cations and metal-binding proteins are endless. They are involved in all crucial cellular activities. Many pathological conditions are related to the problematic metal metabolism. Research in metalloprotein-related topics is therefore rapidly growing, and different aspects of metal-binding proteins progressively enter curricula at Universities and even at the High School level on occasion. However, no key resource providing basic, but comprehensible knowledge on this rapidly expanding field exists. The Encyclopedia of Metalloproteins aims to bridge this gap, and will attempt to cover various aspects of metalloprotein/metalloproteomics and will deal with the different issues related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The goal is to cover exhaustively all catalytically and biologically crucial metal ions and to find at least one interacting protein for other metal ions. The Encyclopedia of Metalloproteins will provide a key resource for advanced undergraduate and graduate students, researchers, instructors, and professors interested in protein science, biochemistry, cell biology, and genetics.
Life sciences. --- Biochemistry. --- Proteomics. --- Cytology. --- Microbial genetics. --- Life Sciences. --- Biochemistry, general. --- Cell Biology. --- Microbial Genetics and Genomics. --- Proteins --- Amino Acids, Peptides, and Proteins --- Chemicals and Drugs --- Metalloproteins --- Biology --- Chemistry --- Health & Biological Sciences --- Physical Sciences & Mathematics --- Biology - General --- Biochemistry --- Biosciences --- Sciences, Life --- Gene Products, Protein --- Gene Proteins --- Protein Gene Products --- Proteins, Gene --- Microorganisms --- Cell biology --- Cellular biology --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Genetics --- Composition --- Cell biology. --- Microbial genomics. --- Microbiology --- Molecular biology --- Medical sciences --- Genomics --- Microbial genetics --- Cells --- Cytologists
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