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Flexible viruses [[electronic resource] ] : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Flexible viruses [[electronic resource] ] : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Autore Uversky Vladimir N
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2012
Descrizione fisica 1 online resource (534 p.)
Disciplina 612/.015756
Altri autori (Persone) LonghiSonia
Collana Wiley series in protein and peptide science
Soggetto topico Viral proteins
ISBN 1-283-31596-3
9786613315960
1-118-13556-3
1-118-13557-1
1-118-13554-7
Classificazione SCI007000
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto FLEXIBLE VIRUSES; CONTENTS; Preface; Introduction to the Wiley Series on Protein and Peptide Science; Contributors; 1 Do Viral Proteins Possess Unique Features?; 2 Functional Role of Structural Disorder in Capsid Proteins; 3 Structural Disorder Within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses; 4 Structural Disorder Within Sendai Virus Nucleoprotein and Phosphoprotein; 5 Structural Disorder in Proteins of the Rhabdoviridae Replication Complex; 6 Structural Disorder in Matrix Proteins of HIV-Related Viruses
7 Structural Disorder in Proteins From Influenza Virus8 Making Order in the Intrinsically Disordered Regions of HIV-1 Vif Protein; 9 Order from Disorder: Structure, Function, and Dynamics of the HIV-1 Transactivator of Transcription; 10 Intrinsically Disordered Domains of Sesbania Mosaic Virus Encoded Proteins; 11 Intrinsic Disorder in Genome-Linked Viral Proteins VPgs of Potyviruses; 12 Intrinsic Disorder in the Human Papillomavirus E7 Protein; 13 The Semliki Forest Virus Capsid Protease is Disordered and Yet Displays Catalytic Activity
14 Core-lations Between Intrinsic Disorder and Multifaceted Activities in Hepatitis C Virus and Related Viruses15 The NS5A Domain II of HCV: Conservation of Intrinsic Disorder in Several Genotypes; 16 Bacteriophage l N Protein Disorder-Order Transitions Upon Interactions with RNA or Proteins; 17 N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure; Index
Record Nr. UNINA-9910141216203321
Uversky Vladimir N  
Hoboken, N.J., : Wiley, c2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Flexible viruses : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Flexible viruses : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Autore Uversky Vladimir N
Edizione [1st ed.]
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2012
Descrizione fisica 1 online resource (534 p.)
Disciplina 612/.015756
Altri autori (Persone) LonghiSonia
Collana Wiley series in protein and peptide science
Soggetto topico Viral proteins
ISBN 1-283-31596-3
9786613315960
1-118-13556-3
1-118-13557-1
1-118-13554-7
Classificazione SCI007000
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto FLEXIBLE VIRUSES; CONTENTS; Preface; Introduction to the Wiley Series on Protein and Peptide Science; Contributors; 1 Do Viral Proteins Possess Unique Features?; 2 Functional Role of Structural Disorder in Capsid Proteins; 3 Structural Disorder Within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses; 4 Structural Disorder Within Sendai Virus Nucleoprotein and Phosphoprotein; 5 Structural Disorder in Proteins of the Rhabdoviridae Replication Complex; 6 Structural Disorder in Matrix Proteins of HIV-Related Viruses
7 Structural Disorder in Proteins From Influenza Virus8 Making Order in the Intrinsically Disordered Regions of HIV-1 Vif Protein; 9 Order from Disorder: Structure, Function, and Dynamics of the HIV-1 Transactivator of Transcription; 10 Intrinsically Disordered Domains of Sesbania Mosaic Virus Encoded Proteins; 11 Intrinsic Disorder in Genome-Linked Viral Proteins VPgs of Potyviruses; 12 Intrinsic Disorder in the Human Papillomavirus E7 Protein; 13 The Semliki Forest Virus Capsid Protease is Disordered and Yet Displays Catalytic Activity
14 Core-lations Between Intrinsic Disorder and Multifaceted Activities in Hepatitis C Virus and Related Viruses15 The NS5A Domain II of HCV: Conservation of Intrinsic Disorder in Several Genotypes; 16 Bacteriophage l N Protein Disorder-Order Transitions Upon Interactions with RNA or Proteins; 17 N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure; Index
Record Nr. UNINA-9910809692803321
Uversky Vladimir N  
Hoboken, N.J., : Wiley, c2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
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
Opac: Controlla la disponibilità qui
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
Opac: Controlla la disponibilità qui
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
Opac: Controlla la disponibilità qui