top

  Info

  • Utilizzare la checkbox di selezione a fianco di ciascun documento per attivare le funzionalità di stampa, invio email, download nei formati disponibili del (i) record.

  Info

  • Utilizzare questo link per rimuovere la selezione effettuata.

Biblioteca

MARC Lista (tabellare)
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 9786613315960
9781283315968
1283315963
9781118135563
1118135563
9781118135570
1118135571
9781118135549
1118135547
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 9786613371522
9781283371520
1283371529
9780470602607
0470602600
9780470602614
0470602619
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-9911020005703321
Hoboken, N.J., : Wiley, c2010
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui