Encyclopedia of Metalloproteins [[electronic resource] /] / edited by Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov |
Edizione | [1st ed. 2013.] |
Pubbl/distr/stampa | New York, NY : , : Springer New York : , : Imprint : Springer, , 2013 |
Descrizione fisica | 1 online resource (LVII, 2574 p. 1108 illus., 777 illus. in color. eReference.) |
Disciplina | 572 |
Soggetto topico |
Biochemistry
Proteomics Cell biology Microbial genetics Microbial genomics Biochemistry, general Cell Biology Microbial Genetics and Genomics |
ISBN | 1-4614-1533-0 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Period 2: Lithium, Beryllium -- Period 3: Sodium, Magnesium, Aluminium -- Period 4: Potassium, Calcium, Scandium, Titanium, Vanadium, Chromium, Manganese, Iron, Cobalt, Nickel, Copper, Zinc, Gallium -- Period 5: Rubidium, Strontium, Yttrium, Zirconium, Niobium, Molybdenum, Technetium, Ruthenium, Rhodium, Palladium, Silver, Cadmium, Indium, Tin -- Period 6: Caesium, Barium, Lanthaninds (Lanthanum, Cerium, Praseodymium, Neodymium, Promethium, Samarium, Europium, Gadolinium, Terbium, Dysprosium, Holmium, Erbium, Thulium, Ytterbium), Lutetium, Hafnium, Tantalum, Wolfram, Rhenium, Osmium, Iridium, Platinum, Gold, Mercury, Thallium, Lead, Bismuth -- Period 7: Francium, Radium, Actinides (Actinium, Thorium, Protactinium, Uranium). |
Record Nr. | UNINA-9910437606103321 |
New York, NY : , : Springer New York : , : Imprint : Springer, , 2013 | ||
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Lo trovi qui: Univ. Federico II | ||
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Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (792 p.) |
Disciplina | 572.633 |
Altri autori (Persone) |
LonghiSonia
UverskyVladimir N |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Analysis
Proteins - Conformation Proteins - Denaturation |
ISBN |
1-283-37152-9
9786613371522 0-470-60260-0 0-470-60261-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
INSTRUMENTAL ANALYSIS OF INTRINSICALLY DISORDERED PROTEINS: Assessing Structure and Conformation; CONTENTS; PREFACE; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; LIST OF CONTRIBUTORS; LIST OF ABBREVIATIONS; PART I: ASSESSING IDPs IN THE LIVING CELL; 1: IDPs AND PROTEIN DEGRADATION IN THE CELL; 2: THE STRUCTURAL BIOLOGY OF IDPs INSIDE CELLS; PART II: SPECTROSCOPIC TECHNIQUES; 3: NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY APPLIED TO (INTRINSICALLY) DISORDERED PROTEINS; 4: ATOMIC-LEVEL CHARACTERIZATION OF DISORDERED PROTEIN ENSEMBLES USING NMR RESIDUAL DIPOLAR COUPLINGS
5: DETERMINING STRUCTURAL ENSEMBLES FOR INTRINSICALLY DISORDERED PROTEINS6: SITE-DIRECTED SPIN LABELING EPR SPECTROSCOPY; 7: THE STRUCTURE OF UNFOLDED PEPTIDES AND PROTEINS EXPLORED BY VIBRATIONAL SPECTROSCOPY; 8: INTRINSICALLY DISORDERED PROTEINS AND INDUCED FOLDING STUDIED BY FOURIER TRANSFORM INFRARED SPECTROSCOPY; 9: GENETICALLY ENGINEERED POLYPEPTIDES AS A MODEL OF INTRINSICALLY DISORDERED FIBRILLOGENIC PROTEINS: DEEP UV RESONANCE RAMAN SPECTROSCOPIC STUDY; 10: CIRCULAR DICHROISM OF INTRINSICALLY DISORDERED PROTEINS; 11: FLUORESCENCE SPECTROSCOPY OF INTRINSICALLY DISORDERED PROTEINS 12: HYDRATION OF INTRINSICALLY DISORDERED PROTEINS FROM WIDE-LINE NMRPART III: SINGLE-MOLECULE TECHNIQUES; 13: SINGLE-MOLECULE SPECTROSCOPY OF UNFOLDED PROTEINS; 14: MONITORING THE CONFORMATIONAL EQUILIBRIA OF MONOMERIC INTRINSICALLY DISORDERED PROTEINS BY SINGLE-MOLECULE FORCE SPECTROSCOPY; PART IV: METHODS TO ASSESS PROTEIN SIZE AND SHAPE; 15: ANALYTICAL ULTRACENTRIFUGATION, A USEFUL TOOL TO PROBE INTRINSICALLY DISORDERED PROTEINS; 16: STRUCTURAL INSIGHTS INTO INTRINSICALLY DISORDERED PROTEINS BY SMALL-ANGLE X-RAY SCATTERING; 17: DYNAMIC AND STATIC LIGHT SCATTERING 18: ANALYZING INTRINSICALLY DISORDERED PROTEINS BY SIZE EXCLUSION CHROMATOGRAPHYPART V: CONFORMATIONAL STABILITY; 19: CONFORMATIONAL BEHAVIOR OF INTRINSICALLY DISORDERED PROTEINS: EFFECTS OF STRONG DENATURANTS, TEMPERATURE, PH , COUNTERIONS, AND MACROMOLECULAR CROWDING; 20: DETECTING DISORDERED REGIONS IN PROTEINS BY LIMITED PROTEOLYSIS; PART VI: MASS SPECTROMETRY; 21: MASS SPECTROMETRY TOOLS FOR THE INVESTIGATION OF STRUCTURAL DISORDER AND CONFORMATIONAL TRANSITIONS IN PROTEINS; PART VII: EXPRESSION AND PURIFICATION OF IDPS 22: RECOMBINANT PRODUCTION OF INTRINSICALLY DISORDERED PROTEINS FOR BIOPHYSICAL AND STRUCTURAL CHARACTERIZATION23: LARGE-SCALE IDENTIFICATION OF INTRINSICALLY DISORDERED PROTEINS; 24: PURIFICATION OF INTRINSICALLY DISORDERED PROTEINS; INDEX; Colour plates |
Record Nr. | UNINA-9910139407003321 |
Hoboken, N.J., : Wiley, c2010 | ||
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Lo trovi qui: Univ. Federico II | ||
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Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (792 p.) |
Disciplina | 572.633 |
Altri autori (Persone) |
LonghiSonia
UverskyVladimir N |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Analysis
Proteins - Conformation Proteins - Denaturation |
ISBN |
1-283-37152-9
9786613371522 0-470-60260-0 0-470-60261-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
INSTRUMENTAL ANALYSIS OF INTRINSICALLY DISORDERED PROTEINS: Assessing Structure and Conformation; CONTENTS; PREFACE; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; LIST OF CONTRIBUTORS; LIST OF ABBREVIATIONS; PART I: ASSESSING IDPs IN THE LIVING CELL; 1: IDPs AND PROTEIN DEGRADATION IN THE CELL; 2: THE STRUCTURAL BIOLOGY OF IDPs INSIDE CELLS; PART II: SPECTROSCOPIC TECHNIQUES; 3: NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY APPLIED TO (INTRINSICALLY) DISORDERED PROTEINS; 4: ATOMIC-LEVEL CHARACTERIZATION OF DISORDERED PROTEIN ENSEMBLES USING NMR RESIDUAL DIPOLAR COUPLINGS
5: DETERMINING STRUCTURAL ENSEMBLES FOR INTRINSICALLY DISORDERED PROTEINS6: SITE-DIRECTED SPIN LABELING EPR SPECTROSCOPY; 7: THE STRUCTURE OF UNFOLDED PEPTIDES AND PROTEINS EXPLORED BY VIBRATIONAL SPECTROSCOPY; 8: INTRINSICALLY DISORDERED PROTEINS AND INDUCED FOLDING STUDIED BY FOURIER TRANSFORM INFRARED SPECTROSCOPY; 9: GENETICALLY ENGINEERED POLYPEPTIDES AS A MODEL OF INTRINSICALLY DISORDERED FIBRILLOGENIC PROTEINS: DEEP UV RESONANCE RAMAN SPECTROSCOPIC STUDY; 10: CIRCULAR DICHROISM OF INTRINSICALLY DISORDERED PROTEINS; 11: FLUORESCENCE SPECTROSCOPY OF INTRINSICALLY DISORDERED PROTEINS 12: HYDRATION OF INTRINSICALLY DISORDERED PROTEINS FROM WIDE-LINE NMRPART III: SINGLE-MOLECULE TECHNIQUES; 13: SINGLE-MOLECULE SPECTROSCOPY OF UNFOLDED PROTEINS; 14: MONITORING THE CONFORMATIONAL EQUILIBRIA OF MONOMERIC INTRINSICALLY DISORDERED PROTEINS BY SINGLE-MOLECULE FORCE SPECTROSCOPY; PART IV: METHODS TO ASSESS PROTEIN SIZE AND SHAPE; 15: ANALYTICAL ULTRACENTRIFUGATION, A USEFUL TOOL TO PROBE INTRINSICALLY DISORDERED PROTEINS; 16: STRUCTURAL INSIGHTS INTO INTRINSICALLY DISORDERED PROTEINS BY SMALL-ANGLE X-RAY SCATTERING; 17: DYNAMIC AND STATIC LIGHT SCATTERING 18: ANALYZING INTRINSICALLY DISORDERED PROTEINS BY SIZE EXCLUSION CHROMATOGRAPHYPART V: CONFORMATIONAL STABILITY; 19: CONFORMATIONAL BEHAVIOR OF INTRINSICALLY DISORDERED PROTEINS: EFFECTS OF STRONG DENATURANTS, TEMPERATURE, PH , COUNTERIONS, AND MACROMOLECULAR CROWDING; 20: DETECTING DISORDERED REGIONS IN PROTEINS BY LIMITED PROTEOLYSIS; PART VI: MASS SPECTROMETRY; 21: MASS SPECTROMETRY TOOLS FOR THE INVESTIGATION OF STRUCTURAL DISORDER AND CONFORMATIONAL TRANSITIONS IN PROTEINS; PART VII: EXPRESSION AND PURIFICATION OF IDPS 22: RECOMBINANT PRODUCTION OF INTRINSICALLY DISORDERED PROTEINS FOR BIOPHYSICAL AND STRUCTURAL CHARACTERIZATION23: LARGE-SCALE IDENTIFICATION OF INTRINSICALLY DISORDERED PROTEINS; 24: PURIFICATION OF INTRINSICALLY DISORDERED PROTEINS; INDEX; Colour plates |
Record Nr. | UNINA-9910830708903321 |
Hoboken, N.J., : Wiley, c2010 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (792 p.) |
Disciplina | 572.633 |
Altri autori (Persone) |
LonghiSonia
UverskyVladimir N |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Analysis
Proteins - Conformation Proteins - Denaturation |
ISBN |
1-283-37152-9
9786613371522 0-470-60260-0 0-470-60261-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
INSTRUMENTAL ANALYSIS OF INTRINSICALLY DISORDERED PROTEINS: Assessing Structure and Conformation; CONTENTS; PREFACE; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; LIST OF CONTRIBUTORS; LIST OF ABBREVIATIONS; PART I: ASSESSING IDPs IN THE LIVING CELL; 1: IDPs AND PROTEIN DEGRADATION IN THE CELL; 2: THE STRUCTURAL BIOLOGY OF IDPs INSIDE CELLS; PART II: SPECTROSCOPIC TECHNIQUES; 3: NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY APPLIED TO (INTRINSICALLY) DISORDERED PROTEINS; 4: ATOMIC-LEVEL CHARACTERIZATION OF DISORDERED PROTEIN ENSEMBLES USING NMR RESIDUAL DIPOLAR COUPLINGS
5: DETERMINING STRUCTURAL ENSEMBLES FOR INTRINSICALLY DISORDERED PROTEINS6: SITE-DIRECTED SPIN LABELING EPR SPECTROSCOPY; 7: THE STRUCTURE OF UNFOLDED PEPTIDES AND PROTEINS EXPLORED BY VIBRATIONAL SPECTROSCOPY; 8: INTRINSICALLY DISORDERED PROTEINS AND INDUCED FOLDING STUDIED BY FOURIER TRANSFORM INFRARED SPECTROSCOPY; 9: GENETICALLY ENGINEERED POLYPEPTIDES AS A MODEL OF INTRINSICALLY DISORDERED FIBRILLOGENIC PROTEINS: DEEP UV RESONANCE RAMAN SPECTROSCOPIC STUDY; 10: CIRCULAR DICHROISM OF INTRINSICALLY DISORDERED PROTEINS; 11: FLUORESCENCE SPECTROSCOPY OF INTRINSICALLY DISORDERED PROTEINS 12: HYDRATION OF INTRINSICALLY DISORDERED PROTEINS FROM WIDE-LINE NMRPART III: SINGLE-MOLECULE TECHNIQUES; 13: SINGLE-MOLECULE SPECTROSCOPY OF UNFOLDED PROTEINS; 14: MONITORING THE CONFORMATIONAL EQUILIBRIA OF MONOMERIC INTRINSICALLY DISORDERED PROTEINS BY SINGLE-MOLECULE FORCE SPECTROSCOPY; PART IV: METHODS TO ASSESS PROTEIN SIZE AND SHAPE; 15: ANALYTICAL ULTRACENTRIFUGATION, A USEFUL TOOL TO PROBE INTRINSICALLY DISORDERED PROTEINS; 16: STRUCTURAL INSIGHTS INTO INTRINSICALLY DISORDERED PROTEINS BY SMALL-ANGLE X-RAY SCATTERING; 17: DYNAMIC AND STATIC LIGHT SCATTERING 18: ANALYZING INTRINSICALLY DISORDERED PROTEINS BY SIZE EXCLUSION CHROMATOGRAPHYPART V: CONFORMATIONAL STABILITY; 19: CONFORMATIONAL BEHAVIOR OF INTRINSICALLY DISORDERED PROTEINS: EFFECTS OF STRONG DENATURANTS, TEMPERATURE, PH , COUNTERIONS, AND MACROMOLECULAR CROWDING; 20: DETECTING DISORDERED REGIONS IN PROTEINS BY LIMITED PROTEOLYSIS; PART VI: MASS SPECTROMETRY; 21: MASS SPECTROMETRY TOOLS FOR THE INVESTIGATION OF STRUCTURAL DISORDER AND CONFORMATIONAL TRANSITIONS IN PROTEINS; PART VII: EXPRESSION AND PURIFICATION OF IDPS 22: RECOMBINANT PRODUCTION OF INTRINSICALLY DISORDERED PROTEINS FOR BIOPHYSICAL AND STRUCTURAL CHARACTERIZATION23: LARGE-SCALE IDENTIFICATION OF INTRINSICALLY DISORDERED PROTEINS; 24: PURIFICATION OF INTRINSICALLY DISORDERED PROTEINS; INDEX; Colour plates |
Record Nr. | UNINA-9910841226503321 |
Hoboken, N.J., : Wiley, c2010 | ||
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Lo trovi qui: Univ. Federico II | ||
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Intrinsically Disordered Proteins and Chronic Diseases |
Autore | Kulkarni Prakash |
Pubbl/distr/stampa | Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2021 |
Descrizione fisica | 1 electronic resource (224 p.) |
Soggetto topico | Research & information: general |
Soggetto non controllato |
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 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910557746903321 |
Kulkarni Prakash
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Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2021 | ||
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Lo trovi qui: Univ. Federico II | ||
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