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DNA-protein interactions --- DNA-proteïneinteracties --- Interactions ADN-protéine --- DNA-Binding Proteins --- Biological techniques --- Enzymology --- Molecular biology --- DNA --- Proteins --- ADN --- Protéines --- analysis.

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Conferences - Meetings --- Zinc-finger proteins --- DNA-protein interactions --- Transcription factors --- Genetic regulation --- Carcinogenesis --- Zinc fingers --- Zinc proteins --- Genetic transcription factors --- Proteins --- DNA-protein binding --- Interactions, DNA-protein --- Protein-DNA interactions --- DNA-ligand interactions --- Protein binding --- Congresses --- DNA-Binding Proteins. --- Zinc-finger proteins - Congresses. --- DNA-protein interactions - Congresses. --- Carcinogenesis - Congresses. --- Transcription factors - Congresses. --- Genetic regulation - Congresses. --- Transcription, genetic

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This book presents a concise overview of current research on the biophysics of DNA-protein interactions. A wide range of new and classical methods are presented by authors investigating physical mechanisms by which proteins interact with DNA. For example, several chapters address the mechanisms by which proteins search for and recognize specific binding sites on DNA, a process critical for cellular function. Single molecule methods such as force spectroscopy as well as fluorescence imaging and tracking are described in these chapters as well as other parts of the book that address the dynamics of protein-DNA interactions. Other important topics include the mechanisms by which proteins engage DNA sequences and/or alter DNA structure. These simple but important model interactions are then placed in the broader biological context with discussion of larger protein-DNA complexes . Topics include replication forks, recombination complexes, DNA repair interactions, and ultimately, methods to understand the chromatin context of the cell nucleus. This book will be of interest to readers who wish to explore current biophysical approaches to DNA-protein interactions across multiple levels of biological complexity.

DNA-protein interactions. --- DNA-protein interactions --- Molecular biology --- Physical Phenomena --- Proteins --- Phenomena and Processes --- Amino Acids, Peptides, and Proteins --- DNA-Binding Proteins --- Biophysical Phenomena --- Chemicals and Drugs --- Human Anatomy & Physiology --- Biology --- Health & Biological Sciences --- Animal Biochemistry --- Biophysics --- Molecular biology. --- Molecular biochemistry --- Molecular biophysics --- DNA-protein binding --- Interactions, DNA-protein --- Protein-DNA interactions --- Physics. --- Biochemistry. --- Proteins. --- Cell biology. --- Biophysics. --- Biological physics. --- Biomedical engineering. --- Biophysics and Biological Physics. --- Molecular Medicine. --- Cell Biology. --- Biomedical Engineering. --- Biochemistry, general. --- Protein Structure. --- Biochemistry --- Biomolecules --- Systems biology --- DNA-ligand interactions --- Protein binding --- Medicine. --- Cytology. --- Biological and Medical Physics, Biophysics. --- Biomedical Engineering and Bioengineering. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Clinical engineering --- Medical engineering --- Bioengineering --- Engineering --- Medicine --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Composition --- Health Workforce --- Proteins . --- Proteids --- Polypeptides --- Proteomics --- Biological physics --- Physics

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DNA-protein interactions --- DNA-Binding Proteins --- DNA Footprinting --- genetics --- methods --- chemistry --- Biochemistry --- Biotechnology --- Human genetics --- Medicine --- Microbiology --- Interactions ADN-protéine --- Biology. --- DNA-protein interactions. --- Electronic books. -- local. --- Proteins --- Nuclease Protection Assays --- Genetic Techniques --- Investigative Techniques --- Amino Acids, Peptides, and Proteins --- Chemicals and Drugs --- Analytical, Diagnostic and Therapeutic Techniques and Equipment --- Human Anatomy & Physiology --- Health & Biological Sciences --- Mechanical Engineering --- Engineering & Applied Sciences --- Animal Biochemistry --- Bioengineering --- Biomedical Engineering --- DNA-protein binding --- Interactions, DNA-protein --- Protein-DNA interactions --- Chemistry. --- Medical microbiology. --- Analytical chemistry. --- Biotechnology. --- Genetic engineering. --- Medicinal chemistry. --- Biochemistry. --- Genetic Engineering. --- Biochemistry, general. --- Analytical Chemistry. --- Medical Microbiology. --- Medicinal Chemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Chemistry, Medical and pharmaceutical --- Chemistry, Pharmaceutical --- Drug chemistry --- Drugs --- Medical chemistry --- Medicinal chemistry --- Pharmacochemistry --- Designed genetic change --- Engineering, Genetic --- Gene splicing --- Genetic intervention --- Genetic surgery --- Genetic recombination --- Transgenic organisms --- Chemical engineering --- Genetic engineering --- Analysis, Chemical --- Analytical chemistry --- Chemical analysis --- Metallurgical analysis --- Mineralogy, Determinative --- Physical sciences --- Composition --- Life sciences --- Biomass --- Life (Biology) --- Natural history --- DNA-ligand interactions --- Protein binding --- Analytical biochemistry. --- Microbiology. --- Microbial biology --- Microorganisms --- Analytic biochemistry --- Chemistry, Analytic --- Bioanalytic chemistry --- Bioanalytical chemistry --- Analytic chemistry

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Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. Recently, however, evidence has emerged for a new type of disordered protein family whose members can undergo coupled folding and binding without the involvement of any folded proteins. Instead, they interact with each other, stabilizing their structure via “mutual synergistic folding” and, surprisingly, they exhibit the same residue composition as the folded protein. Increasingly more examples have been found where disordered proteins interact with non-protein macromolecules, adding to the already large variety of protein–protein interactions. There is also a very new phenomenon when proteins are involved in phase separation, which can represent a weak but functionally important macromolecular interaction. These phenomena are presented and discussed in the chapters of this book.

Research & information: general --- Biology, life sciences --- intrinsically disordered proteins --- epiproteome --- disordered protein platform --- molecular recognition feature --- post-translational modifications --- physiological homeostasis --- stress response --- RIN4 --- p53 --- molecular machines --- intrinsically disordered protein --- membrane-less organelle --- neurodegenerative disease --- p300 HAT acetylation --- post-translational modification --- protein aggregation --- Tau fibrillation --- intrinsically disorder proteins --- disorder-to-order regions --- protein–RNA interactions --- unstructured proteins --- conformational plasticity --- disordered protein --- folding --- ribosomal protein --- spectroscopy --- protein stability --- temperature response --- protein thermostability --- salt bridges --- meta strategy --- dual threshold --- significance voting --- decision tree based artificial neural network --- protein intrinsic disorder --- intrinsic disorder --- intrinsic disorder prediction --- intrinsically disordered region --- protein conformation --- transcriptome --- RNA sequencing --- Microarray --- differentially regulated genes --- gene ontology analysis --- functional analysis --- intrinsically disordered --- structural disorder --- correlated mutations --- co-evolution --- evolutionary couplings --- residue co-variation --- interaction surface --- residue contact network --- dehydron --- homodimer --- hydrogen bond --- inter-subunit interaction --- ion pair --- mutual synergistic folding --- solvent-accessible surface area --- stabilization center --- MLL proteins --- MLL4 --- lncRNA --- HOTAIR --- MEG3 --- leukemia --- histone lysine methyltransferase --- RNA binding --- protein --- hydration --- wide-line 1H NMR --- secretion --- immune --- extracellular --- protein-protein interaction --- structural domain --- evolution --- transcription factors --- DNA-protein interactions --- Sox2 sequential DNA loading --- smFRET --- DNA conformational landscape --- sequential DNA bending --- transcription factor dosage --- oligomer --- N-terminal prion protein --- copper binding --- prion disease mutations --- Nuclear pore complex --- FG-Nups --- phosphorylation --- coarse-grained --- CABS model --- MC simulations --- statistical force fields --- protein structure --- intrinsically disordered proteins (IDPs) --- neurodegenerative diseases --- aggregation --- drugs --- drug discovery --- plant virus --- eIF4E --- VPg --- potyvirus --- molten globule --- fluorescence anisotropy --- protein hydrodynamics --- intrinsically disordered proteins --- epiproteome --- disordered protein platform --- molecular recognition feature --- post-translational modifications --- physiological homeostasis --- stress response --- RIN4 --- p53 --- molecular machines --- intrinsically disordered protein --- membrane-less organelle --- neurodegenerative disease --- p300 HAT acetylation --- post-translational modification --- protein aggregation --- Tau fibrillation --- intrinsically disorder proteins --- disorder-to-order regions --- protein–RNA interactions --- unstructured proteins --- conformational plasticity --- disordered protein --- folding --- ribosomal protein --- spectroscopy --- protein stability --- temperature response --- protein thermostability --- salt bridges --- meta strategy --- dual threshold --- significance voting --- decision tree based artificial neural network --- protein intrinsic disorder --- intrinsic disorder --- intrinsic disorder prediction --- intrinsically disordered region --- protein conformation --- transcriptome --- RNA sequencing --- Microarray --- differentially regulated genes --- gene ontology analysis --- functional analysis --- intrinsically disordered --- structural disorder --- correlated mutations --- co-evolution --- evolutionary couplings --- residue co-variation --- interaction surface --- residue contact network --- dehydron --- homodimer --- hydrogen bond --- inter-subunit interaction --- ion pair --- mutual synergistic folding --- solvent-accessible surface area --- stabilization center --- MLL proteins --- MLL4 --- lncRNA --- HOTAIR --- MEG3 --- leukemia --- histone lysine methyltransferase --- RNA binding --- protein --- hydration --- wide-line 1H NMR --- secretion --- immune --- extracellular --- protein-protein interaction --- structural domain --- evolution --- transcription factors --- DNA-protein interactions --- Sox2 sequential DNA loading --- smFRET --- DNA conformational landscape --- sequential DNA bending --- transcription factor dosage --- oligomer --- N-terminal prion protein --- copper binding --- prion disease mutations --- Nuclear pore complex --- FG-Nups --- phosphorylation --- coarse-grained --- CABS model --- MC simulations --- statistical force fields --- protein structure --- intrinsically disordered proteins (IDPs) --- neurodegenerative diseases --- aggregation --- drugs --- drug discovery --- plant virus --- eIF4E --- VPg --- potyvirus --- molten globule --- fluorescence anisotropy --- protein hydrodynamics