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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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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 --- 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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Protein folding --- Protein Folding. --- 577.122 --- Folding of proteins --- Proteins --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Protein Multimerization --- Intrinsically Disordered Proteins --- Protein metabolism --- Folding --- Conformation --- 577.122 Protein metabolism --- Protein Folding --- Proteostasis --- Protein folding. --- Kinetics

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The past five years have seen a major leap forward in our understanding of the way proteins fold into their three-dimensional, functional conformations. The rapidly expanding literature covers in vivo as well as in vitro studies and forms the basis for an important biotechnology industry. In this volume, a group of leading scientists review and assess the experimental evidence that underpins these advances and look for signs of a general picture of how proteins fold. Contributors show how such conformational changes are leading to new insights into membrane translocation, pore formation, and the clinically important aggregation phenomena. Students and researchers of biochemistry and molecular biology will find this book to be the ideal introduction to an exciting field.

General biophysics --- Molecular biology --- Macromolecules --- Protein folding --- Protéines --- Repliement --- Protein Folding. --- Folding of proteins --- Proteins --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Protein Multimerization --- Intrinsically Disordered Proteins --- Folding --- Conformation --- Protein folding. --- Protéines --- Protein Folding --- Proteostasis --- fysicochemie

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Prions --- Protein folding --- Prions. --- Protein folding. --- Folding of proteins --- Proteins --- Infectious protein particles --- Prion proteins --- Protein particles, Infectious --- Proteinaceous infection particles --- PrP proteins --- Folding --- Protein Folding --- Conformation --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Proteostasis --- Protein Multimerization --- Intrinsically Disordered Proteins --- Mink Encephalopathy Virus --- Encephalopathy Virus, Mink --- Scrapie --- Agriculture Sciences --- Soil Chemistry, Microbiology, Fertility & Fertilizers --- Prion --- protein folding --- protein assembly disorders --- prion diseases --- prions --- Protein Folding.