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Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Instrumental analysis of intrinsically disordered proteins : assessing structure and conformation / / edited by Vladimir N. Uversky and Sonia Longhi
| 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-9910877552603321 |
| Hoboken, N.J., : Wiley, c2010 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein aggregation [[electronic resource] /] / Douglas A. Stein, editor
| Protein aggregation [[electronic resource] /] / Douglas A. Stein, editor |
| Pubbl/distr/stampa | New York, : Nova Biomedical Books, c2011 |
| Descrizione fisica | 1 online resource (312 p.) |
| Disciplina | 572/.633 |
| Altri autori (Persone) | SteinDouglas A |
| Collana |
Protein science and engineering
Microbiology research advances |
| Soggetto topico |
Proteins - Denaturation
Protein folding |
| Soggetto genere / forma | Electronic books. |
| ISBN | 1-61122-126-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910452737903321 |
| New York, : Nova Biomedical Books, c2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein aggregation [[electronic resource] /] / Douglas A. Stein, editor
| Protein aggregation [[electronic resource] /] / Douglas A. Stein, editor |
| Pubbl/distr/stampa | New York, : Nova Biomedical Books, c2011 |
| Descrizione fisica | 1 online resource (312 p.) |
| Disciplina | 572/.633 |
| Altri autori (Persone) | SteinDouglas A |
| Collana |
Protein science and engineering
Microbiology research advances |
| Soggetto topico |
Proteins - Denaturation
Protein folding |
| ISBN | 1-61122-126-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910779647503321 |
| New York, : Nova Biomedical Books, c2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein aggregation / / Douglas A. Stein, editor
| Protein aggregation / / Douglas A. Stein, editor |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | New York, : Nova Biomedical Books, c2011 |
| Descrizione fisica | 1 online resource (312 p.) |
| Disciplina | 572/.633 |
| Altri autori (Persone) | SteinDouglas A |
| Collana |
Protein science and engineering
Microbiology research advances |
| Soggetto topico |
Proteins - Denaturation
Protein folding |
| ISBN | 1-61122-126-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Intro -- PROTEIN AGGREGATION -- PROTEIN AGGREGATION -- Contents -- Preface -- Changes in Protein Structure under the Effects of Cryopreservation and Cryoprotective Agents -- Abstract -- Introduction -- Cold Denaturation of Proteins -- Disturbance of Protein Conformation Affected by Ice Formation -- Disturbance of Protein Conformation Affected by Dehydration -- Stabilizing Effects of Cryopotectant Agents on Proteins -- Aggregation Frozen-Thawed and Frozen-Dried Proteins -- Conclusion -- References -- Molecular Chaperones and Proteases as Suppressors of Protein Aggregation in Gram-Negative Bacteria -- Abstract -- Introduction -- The Cytoplasmic Protein Quality Control Systems -- Cytoplasmic Chaperones -- Hsp70 System -- Hsp60 System -- HtpG (Hsp90) -- sHsps -- Hsp100 -- Protein Unfolding and Degradation -- Proteolysis in the Bacterial Cytoplasm -- Structural Features of AAA+ Proteases -- Mechanisms of Substrate Recognition -- Proteolysis as a Control Mechanism under Stressful Conditions -- Role of Molecular Chaperones and Proteases in the Cytoplasmic Inclusion Bodies Processing -- The Extracytoplasmic Protein Quality Control Systems -- Skp -- SurA -- FkpA -- Acid-Stress Chaperones HdeA and HdeB -- Periplasmic Proteases -- HtrA -- Characterization of the Proteolytic Activity of HtrA -- Characterization of the Chaperone Activity of HtrA -- Other Extracytoplasmic Proteases -- Expression of Recombinant Proteins in the Periplasm - Troubleshooting -- Conclusion -- References -- Native Functions of Amyloid -- Abstract -- Introduction -- 1. Functional Amyloids -- 22. Bacteerial Ammyloid -- 2.1. Curli Fibrils -- 2.2. Pili of Mycobacterium Tuberculosis -- 2.3. Chaplin Fibrils -- 2.4. Microcin Amyloid -- 2.5. Harpins of Plant Pathogenic Bacteria -- 2.6. Endospore -- 2.7. Biofilms -- 2.8. Bacterial Inclusion Bodies Contain Amyloid Like Structure.
3. Fungal Amyloid -- 3.1. Hydrophobins -- 3.1.1. SC3 Hydrophobin -- 3.1.2. EAS of Neurospora Crassa -- 3.2. Adhesins of Yeast -- 4. Fungal Prions -- 4.1. Het-s amyloid in Podospora anserine -- 4.2. Yeast Prions -- 4.2.1. Amyloid of Ure2p in [URE3] -- 4.2.2. Amyloid of Sup35 in [PSI+] -- 4.2.3. Amyloid of Rnq1 in [PIN+] -- 5. Mammalian Functional Amyloid -- 5.1. Biogenesis of Mammalian Melanosome -- 5.1.1. Pmel Amyloid and Melanin Synthesis -- 5.2. Amyloid in Secretory Granules Biogenesis -- 6. Other Functional Amyloids -- 7. Functional vs Disease Amyloid -- 8. Conclusion and Future Direction -- Acknowledgment -- References -- Nucleation Mechanisms and Morphologies in Insulin Amyloid Fibril Formation -- Abstract -- 1. Introduction -- 1.1. Nucleation Mechanisms in Protein Aggregation -- 1.1.1. Homogeneous and Secondary Nucleation -- 1.2. Model System, Experimental Approach and Aim of the Study -- 2. Results and Discussion -- 2.1. Human Insulin in Acetic Acid Solutions -- 2.1.1. Characterization of Fibril Formation -- 2.1.2. Correlation between FFV and 1/t50% -- 2.1.3. Statistical Study -- 2.2. Bovine insulin in HCl Solutions -- 2.2.1 Different Processes and Morphologies Occurring during the Fibrillation Kinetics -- 2.2.2. Lag Phase in the Low Concentration Regime -- 2.2.3. Initial Fibrils Growth in the Low Concentration Regime -- Conclusions -- Acknowledgments -- References -- On the Aggregation of Albumin: Influences of the Protein Glycation -- Abstract -- Introduction -- Importance of Albumin in Human Physiology -- Structural Aspect of Albumin -- Albumin Aggregation -- BSA Structural Modifications and Aggregation -- Albumin Aggregation - Consequences of the Protein Glycation -- Albumin Glycation Impact on Albumin Structure -- Albumin Glycation is Characterized by Aggregates Growth -- Glycated Albumin Showed Lower Propensity For Thermal Aggregation. Conclusion -- Acknowledgments -- References -- The Role of Conformational Domain Lability of Fibrinogen Molecules in Processes of Self-Assembly of Fibrin Monomers and Fibrinogen Aggregation -- Abstract -- Introduction -- The Self-Assembly of the Single-Stranded Fibrin Protofibrils -- Mechanism of Aggregation of Fibrinogen Molecules. The Influence of Fibrin-Stabilizing Factor -- Structural Modification of Fibrinogen as a Result of Free-Radical Oxidation -- References -- Two Faced Members of the Family: The Synucleins -- Abstract -- Introduction -- Physiological Functions of Synucleins -- α-Synuclein -- β-Synuclein -- γ-Synuclein -- Interaction of Amyloidogenic Proteins -- Oxidized γ-synuclein is Toxic and Acts as an Antichaperone -- Conclusion -- Acknowledgment -- References -- Inclusion Bodies: A New Concept of Biocatalysts -- Acknowledgments -- References -- Comparative Study of Bovine and Ovine Caseinate Aggregation Processes: Calcium-Induced Aggregation and Acid Aggregation -- Abstract -- Introduction -- Colloidal Stability Test -- Size Variations of the CCA -- Analysis of Conformational and Surface Hydrophobicity Changes -- Caseinate Acid Aggregation -- Rheological Properties of Acid Gels -- Conclusion -- References -- Protein Aggregation -- Abstract -- Introduction -- Protein Aggregation and Neurodegenerative Disease -- Protein Folding in Solution -- Many Factors Affect the Protein Aggregation Process -- Protein Aggregation and Cytotoxicity -- Conclusion -- Acknowledgments -- References -- Yeast Protein Aggregates, Containing Chaperones and Glucose Metabolism Enzymes -- Abstract -- Introduction -- Materials and Methods -- Strains and Pasmids -- The Cultural Media and Basic Methods -- Preparation and Analysis of Cell Lysate Pellets -- Electrophoresis -- Measuring Fluorescence Intensity -- Model Experiments with Insulin Fibrils. Red Pigment purification -- Two-dimensional Polyacrylamide Gel Electrophoresis -- Mass spectrometry and Protein Identification -- Results -- Conclusion -- Acknowledgments -- References -- Folding and Aggregation Features of Proteins -- Abstract -- Introduction -- Results and Discussion -- A Description of the Database of Globular Proteins with Experimentally Determined Amyloidogenic Regions -- Theoretical Search for Folding Nuclei of Amyloidogenic Proteins -- Intersection of Experimentally Determined Amyloidogenic Regions with the Predicted Folding Nuclei -- Materials and Methods -- Creation of the Database of Amyloidogenic Proteins -- Theoretical Search for Folding Nuclei -- Calculation of Φ-Values -- Statistical Tests -- Acknowledgments -- Funding -- References -- Chapter Sources -- Index. |
| Record Nr. | UNINA-9910816620703321 |
| New York, : Nova Biomedical Books, c2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
