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Louis Sullivan (1856 - 1924) revolutionized architecture by designing the first skyscraper and he became famous by proclaiming that “form follows function”. When x-ray crystallographers visualized the structures of proteins for the first time, the structural biology field embraced the view that “function follows form” as the 3D-architecture of proteins could unveil various aspects of their function. Despite the original “1 gene - 1 protein structure - 1 function” relationship, nowadays a far more complicated picture emerges where the flexibility and dynamics of a protein can play a central role in a multitude of functions. The ultimate form(s) that a protein adopt when interacting with (a) partner molecule(s) are the most biologically relevant and in this context Sullivan’s quote is still appropriate: the conformation that the protein adopts follows from the function of that protein. Despite the fact that many well-characterized proteins have a well-folded structure, there is a growing interest in the conformational flexibility within proteins. This flexibility is also a balanced phenomenon: excess of flexibility can be detrimental for protein behaviour, as well as the lack thereof. Notwithstanding its importance, studying intrinsically disordered protein regions or conformational rearrangements can be a very challenging. Therefore, flexibility can be perceived as a friend or a foe, depending on the context. This e-book showcases the impact of the study of protein flexibility on the structural biology field and presents protein flexibility in the context of disease as well as its benign aspects. As detailed knowledge of the structural aspects of polypeptides remains essential to comprehend protein function, one of the future challenges for structural biology also lies with large macromolecular protein complexes. Also there the dynamics and flexibility are essential for proper functioning and molecular movement, which is an important aspect of living matter. This challenge stimulated the development of advanced techniques to study protein flexibility and the use of those techniques to address fundamental biological and biomedical problems. Those innovations should help us to unravel the intimate link between protein function and flexibility and explore new horizons.

conformational selection and induced fit --- protein structure --- conformational ensemble --- Protein function --- protein dynamics --- Protein Conformation --- protein flexibility --- Protein Disorder --- intrinsically disordered proteins --- Structural transition

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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

Research & information: general --- 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

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

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

Research & information: general --- 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