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The chemical biology of nucleic acids / / edited by Gunter Mayer
The chemical biology of nucleic acids / / edited by Gunter Mayer
Edizione [1st ed.]
Pubbl/distr/stampa Chichester, UK, : Wiley, 2010
Descrizione fisica 1 online resource (496 p.)
Disciplina 572.8
Altri autori (Persone) MayerGunter <1972->
Soggetto topico Nucleic acids
Biomolecules
ISBN 1-282-68356-X
9786612683565
0-470-66400-2
0-470-66401-0
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto The Chemical Biology of Nucleic Acids; Contents; Foreword; Preface; List of Contributors; 1 Chemical Synthesis of Modified RNA; 2 Expansion of the Genetic Alphabet in Nucleic Acids by Creating New Base Pairs; 3 Chemical Biology of DNA Replication: Probing DNA Polymerase Selectivity Mechanisms with Modified Nucleotides; 4 Nucleic Acid-templated Chemistry; 5 Chemical Biology of Peptide Nucleic Acids (PNAs); 6 The Interactions of Small Molecules with DNA and RNA; 7 The Architectural Motifs of Folded RNAs; 8 Genesis and Biological Applications of Locked Nucleic Acids (LNAs)
9 Small Non-coding RNA in Bacteria10 MicroRNA-guided Gene Silencing; 11 Nucleic Acid-based Therapies; 12 Innate Immune Recognition of Nucleic Acids; 13 Light-responsive Nucleic Acids for the Spatiotemporal Control of Biological Processes; 14 DNA Methylation; 15 Frameworks for Programming RNA Devices; 16 RNA as a Catalyst: The Diels-Alderase Ribozyme; 17 Evolving an Understanding of RNA Function by In Vitro Approaches; 18 The Chemical Biology of Aptamers: Synthesis and Applications; 19 Nucleic Acids as Detection Tools; 20 Bacterial Riboswitch Discovery and Analysis; Index; Color Plates
Record Nr. UNINA-9910876829803321
Chichester, UK, : Wiley, 2010
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Autore Nandi Nilashis.
Pubbl/distr/stampa Boca Raton : , : CRC Press, , 2012
Descrizione fisica 1 online resource (200 p.)
Disciplina 372/.33
Soggetto topico Chirality
Biomolecules
Soggetto genere / forma Electronic books.
ISBN 0-429-10586-X
1-283-25749-1
9786613257499
1-4398-4003-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Contents; Preface; Acknowledgments; About the author; List of abbreviations; Chapter 1: Introduction; Chapter 2: Chiral discrimination in the active site of oxidoreductases; Chapter 3: Transferases and chiral discrimination; Chapter 4: Influence of chirality on the hydrolysis reactions within the active site of hydrolases; Chapter 5: Influence of chirality on the reactions in the active site of lyases; Chapter 6: Chiral discrimination in the active site of ligases; Chapter 7: Summary and future directions; Back Cover
Record Nr. UNINA-9910461061803321
Nandi Nilashis.  
Boca Raton : , : CRC Press, , 2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Autore Nandi Nilashis.
Pubbl/distr/stampa Boca Raton : , : CRC Press, , 2012
Descrizione fisica 1 online resource (200 p.)
Disciplina 372/.33
Soggetto topico Chirality
Biomolecules
ISBN 0-429-10586-X
1-283-25749-1
9786613257499
1-4398-4003-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Contents; Preface; Acknowledgments; About the author; List of abbreviations; Chapter 1: Introduction; Chapter 2: Chiral discrimination in the active site of oxidoreductases; Chapter 3: Transferases and chiral discrimination; Chapter 4: Influence of chirality on the hydrolysis reactions within the active site of hydrolases; Chapter 5: Influence of chirality on the reactions in the active site of lyases; Chapter 6: Chiral discrimination in the active site of ligases; Chapter 7: Summary and future directions; Back Cover
Record Nr. UNINA-9910789773603321
Nandi Nilashis.  
Boca Raton : , : CRC Press, , 2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Chirality in biological nanospaces : reactions in active sites / / Nilashis Nandi
Autore Nandi Nilashis.
Pubbl/distr/stampa Boca Raton : , : CRC Press, , 2012
Descrizione fisica 1 online resource (200 p.)
Disciplina 372/.33
Soggetto topico Chirality
Biomolecules
ISBN 0-429-10586-X
1-283-25749-1
9786613257499
1-4398-4003-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Contents; Preface; Acknowledgments; About the author; List of abbreviations; Chapter 1: Introduction; Chapter 2: Chiral discrimination in the active site of oxidoreductases; Chapter 3: Transferases and chiral discrimination; Chapter 4: Influence of chirality on the hydrolysis reactions within the active site of hydrolases; Chapter 5: Influence of chirality on the reactions in the active site of lyases; Chapter 6: Chiral discrimination in the active site of ligases; Chapter 7: Summary and future directions; Back Cover
Record Nr. UNINA-9910810119403321
Nandi Nilashis.  
Boca Raton : , : CRC Press, , 2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Cis-trans isomerization in biochemistry [[electronic resource] /] / edited by Christophe Dugave
Cis-trans isomerization in biochemistry [[electronic resource] /] / edited by Christophe Dugave
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (372 p.)
Disciplina 547.12252
547.7804452
Altri autori (Persone) DugaveChristophe
Soggetto topico Biomolecules
Stereochemistry
Isomerism
Biochemistry
Soggetto genere / forma Electronic books.
ISBN 1-280-72283-5
9786610722839
3-527-60933-4
3-527-60949-0
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto cis-trans Isomerization in Biochemistry; Contents; Preface; List of Contributors; 1 Nomenclature; 2 General Mechanisms of Cis-Trans Isomerization: A Rapid Survey; 2.1 Introduction; 2.2 Homolytic Cis-Trans Isomerization; 2.3 Heterolytic Cis-Trans Isomerization; 3 Mechanisms of Cis-Trans Isomerization around the Carbon-Carbon Double Bonds via the Triplet State; 3.1 A Concept of a Triplet-Excited Region; 3.2 Triplet-State Isomerization in Retinal; 3.2.1 Cis-Trans Isomerization Examined by Electronic Absorption and Raman Spectroscopies and by High-Performance Liquid Chromatography Analysis
3.2.2 Triplet-Excited Region in All-trans-Retinal Shown in Terms of Stretching Force Constants Determined by Raman Spectroscopy and Normal Coordinate Analysis [9]3.2.3 Dynamic Triplet-Excited Region in Retinal As Revealed by Deuteration Effects on the Quantum Yields of Isomerization via the T(1) State (Okumura, Koyama, unpublished results); 3.2.4 Summary and Future Trends; 3.3 Triplet-State Isomerization in β-Carotene and Spheroidene; 3.3.1 Cis-Trans Isomerization in β-Carotene Studied by Electronic Absorption and Raman Spectroscopies and by HPLC Analysis
3.3.2 Cis-Trans Isomerization in Spheroidene Studied by Time-Resolved Absorption Spectroscopy and by HPLC Analysis [17]3.3.3 The Triplet-Excited Region of All-trans-Spheroidene in Solution and the Triplet-State Structure of 15-cis-Spheroidene Bound to the Bacterial Reaction Center Determined by Raman Spectroscopy and Normal Coordinate Analysis [18]; 3.3.3.1 All-trans-Spheroidene in Solution; 3.3.3.2 15-cis-Spheroidene Bound to the Reaction Center
3.3.4 Conformational Changes and the Inversion of Spin-Polarization Identified by Low-Temperature Electron Paramagnetic Resonance Spectroscopy of the Reaction Center-Bound 15-cis-Spheroidene: A Hypothetical Mechanism of Triplet-Energy Dissipation [19]3.3.5 Summary and Future Trends; 3.4 Spectroscopic and Analytical Techniques for Studying Cis-Trans Isomerization in the T(1) State; 3.4.1 Spectroscopic Techniques: Electronic Absorption, Raman, and Magnetic Resonance Spectroscopies; 3.4.2 A Useful Analytical Technique: Singular-Value Decomposition Followed by Global Fitting [23-25]
4 Retinal Binding Proteins4.1 Retinal Chromophore in Rhodopsins; 4.1.1 Specific Color Regulation of the Retinal Chromophore in Protein; 4.1.2 Unique Photochemistry of the Retinal Chromophore in Protein; 4.2 Photoisomerization in Visual Rhodopsins; 4.2.1 Structure and Function of Visual Rhodopsins; 4.2.2 Primary Process in Vision Studied by Ultrafast Spectroscopy; 4.2.3 Structural Changes of the Chromophore and Protein upon Retinal Photoisomerization; 4.3 Photoisomerization in Archaeal Rhodopsins; 4.3.1 Structure and Function of Archaeal Rhodopsin
4.3.2 Primary Process in Bacterial Photosynthesis and Light Sensor Studied by Ultrafast Spectroscopy
Record Nr. UNINA-9910144307703321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Cis-trans isomerization in biochemistry [[electronic resource] /] / edited by Christophe Dugave
Cis-trans isomerization in biochemistry [[electronic resource] /] / edited by Christophe Dugave
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (372 p.)
Disciplina 547.12252
547.7804452
Altri autori (Persone) DugaveChristophe
Soggetto topico Biomolecules
Stereochemistry
Isomerism
Biochemistry
ISBN 1-280-72283-5
9786610722839
3-527-60933-4
3-527-60949-0
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto cis-trans Isomerization in Biochemistry; Contents; Preface; List of Contributors; 1 Nomenclature; 2 General Mechanisms of Cis-Trans Isomerization: A Rapid Survey; 2.1 Introduction; 2.2 Homolytic Cis-Trans Isomerization; 2.3 Heterolytic Cis-Trans Isomerization; 3 Mechanisms of Cis-Trans Isomerization around the Carbon-Carbon Double Bonds via the Triplet State; 3.1 A Concept of a Triplet-Excited Region; 3.2 Triplet-State Isomerization in Retinal; 3.2.1 Cis-Trans Isomerization Examined by Electronic Absorption and Raman Spectroscopies and by High-Performance Liquid Chromatography Analysis
3.2.2 Triplet-Excited Region in All-trans-Retinal Shown in Terms of Stretching Force Constants Determined by Raman Spectroscopy and Normal Coordinate Analysis [9]3.2.3 Dynamic Triplet-Excited Region in Retinal As Revealed by Deuteration Effects on the Quantum Yields of Isomerization via the T(1) State (Okumura, Koyama, unpublished results); 3.2.4 Summary and Future Trends; 3.3 Triplet-State Isomerization in β-Carotene and Spheroidene; 3.3.1 Cis-Trans Isomerization in β-Carotene Studied by Electronic Absorption and Raman Spectroscopies and by HPLC Analysis
3.3.2 Cis-Trans Isomerization in Spheroidene Studied by Time-Resolved Absorption Spectroscopy and by HPLC Analysis [17]3.3.3 The Triplet-Excited Region of All-trans-Spheroidene in Solution and the Triplet-State Structure of 15-cis-Spheroidene Bound to the Bacterial Reaction Center Determined by Raman Spectroscopy and Normal Coordinate Analysis [18]; 3.3.3.1 All-trans-Spheroidene in Solution; 3.3.3.2 15-cis-Spheroidene Bound to the Reaction Center
3.3.4 Conformational Changes and the Inversion of Spin-Polarization Identified by Low-Temperature Electron Paramagnetic Resonance Spectroscopy of the Reaction Center-Bound 15-cis-Spheroidene: A Hypothetical Mechanism of Triplet-Energy Dissipation [19]3.3.5 Summary and Future Trends; 3.4 Spectroscopic and Analytical Techniques for Studying Cis-Trans Isomerization in the T(1) State; 3.4.1 Spectroscopic Techniques: Electronic Absorption, Raman, and Magnetic Resonance Spectroscopies; 3.4.2 A Useful Analytical Technique: Singular-Value Decomposition Followed by Global Fitting [23-25]
4 Retinal Binding Proteins4.1 Retinal Chromophore in Rhodopsins; 4.1.1 Specific Color Regulation of the Retinal Chromophore in Protein; 4.1.2 Unique Photochemistry of the Retinal Chromophore in Protein; 4.2 Photoisomerization in Visual Rhodopsins; 4.2.1 Structure and Function of Visual Rhodopsins; 4.2.2 Primary Process in Vision Studied by Ultrafast Spectroscopy; 4.2.3 Structural Changes of the Chromophore and Protein upon Retinal Photoisomerization; 4.3 Photoisomerization in Archaeal Rhodopsins; 4.3.1 Structure and Function of Archaeal Rhodopsin
4.3.2 Primary Process in Bacterial Photosynthesis and Light Sensor Studied by Ultrafast Spectroscopy
Record Nr. UNINA-9910830730203321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Cis-trans isomerization in biochemistry / / edited by Christophe Dugave
Cis-trans isomerization in biochemistry / / edited by Christophe Dugave
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (372 p.)
Disciplina 547.12252
547.7804452
Altri autori (Persone) DugaveChristophe
Soggetto topico Biomolecules
Stereochemistry
Isomerism
Biochemistry
ISBN 1-280-72283-5
9786610722839
3-527-60933-4
3-527-60949-0
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto cis-trans Isomerization in Biochemistry; Contents; Preface; List of Contributors; 1 Nomenclature; 2 General Mechanisms of Cis-Trans Isomerization: A Rapid Survey; 2.1 Introduction; 2.2 Homolytic Cis-Trans Isomerization; 2.3 Heterolytic Cis-Trans Isomerization; 3 Mechanisms of Cis-Trans Isomerization around the Carbon-Carbon Double Bonds via the Triplet State; 3.1 A Concept of a Triplet-Excited Region; 3.2 Triplet-State Isomerization in Retinal; 3.2.1 Cis-Trans Isomerization Examined by Electronic Absorption and Raman Spectroscopies and by High-Performance Liquid Chromatography Analysis
3.2.2 Triplet-Excited Region in All-trans-Retinal Shown in Terms of Stretching Force Constants Determined by Raman Spectroscopy and Normal Coordinate Analysis [9]3.2.3 Dynamic Triplet-Excited Region in Retinal As Revealed by Deuteration Effects on the Quantum Yields of Isomerization via the T(1) State (Okumura, Koyama, unpublished results); 3.2.4 Summary and Future Trends; 3.3 Triplet-State Isomerization in β-Carotene and Spheroidene; 3.3.1 Cis-Trans Isomerization in β-Carotene Studied by Electronic Absorption and Raman Spectroscopies and by HPLC Analysis
3.3.2 Cis-Trans Isomerization in Spheroidene Studied by Time-Resolved Absorption Spectroscopy and by HPLC Analysis [17]3.3.3 The Triplet-Excited Region of All-trans-Spheroidene in Solution and the Triplet-State Structure of 15-cis-Spheroidene Bound to the Bacterial Reaction Center Determined by Raman Spectroscopy and Normal Coordinate Analysis [18]; 3.3.3.1 All-trans-Spheroidene in Solution; 3.3.3.2 15-cis-Spheroidene Bound to the Reaction Center
3.3.4 Conformational Changes and the Inversion of Spin-Polarization Identified by Low-Temperature Electron Paramagnetic Resonance Spectroscopy of the Reaction Center-Bound 15-cis-Spheroidene: A Hypothetical Mechanism of Triplet-Energy Dissipation [19]3.3.5 Summary and Future Trends; 3.4 Spectroscopic and Analytical Techniques for Studying Cis-Trans Isomerization in the T(1) State; 3.4.1 Spectroscopic Techniques: Electronic Absorption, Raman, and Magnetic Resonance Spectroscopies; 3.4.2 A Useful Analytical Technique: Singular-Value Decomposition Followed by Global Fitting [23-25]
4 Retinal Binding Proteins4.1 Retinal Chromophore in Rhodopsins; 4.1.1 Specific Color Regulation of the Retinal Chromophore in Protein; 4.1.2 Unique Photochemistry of the Retinal Chromophore in Protein; 4.2 Photoisomerization in Visual Rhodopsins; 4.2.1 Structure and Function of Visual Rhodopsins; 4.2.2 Primary Process in Vision Studied by Ultrafast Spectroscopy; 4.2.3 Structural Changes of the Chromophore and Protein upon Retinal Photoisomerization; 4.3 Photoisomerization in Archaeal Rhodopsins; 4.3.1 Structure and Function of Archaeal Rhodopsin
4.3.2 Primary Process in Bacterial Photosynthesis and Light Sensor Studied by Ultrafast Spectroscopy
Record Nr. UNINA-9910877550303321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Competitive strategies in life sciences / / Basanta Kumara Behera, Ram Prasad, Shyambhavee Behera
Competitive strategies in life sciences / / Basanta Kumara Behera, Ram Prasad, Shyambhavee Behera
Autore Behera Basanta Kumara
Edizione [1st ed. 2020.]
Pubbl/distr/stampa Singapore : , : Springer, , [2020]
Descrizione fisica 1 online resource (XV, 189 p. 84 illus., 56 illus. in color.)
Disciplina 574.19283
Collana New Paradigms of Living Systems
Soggetto topico Biomolecules
Molecular biology
Nucleic acids
ISBN 981-15-7590-8
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Chapter 1. Strategies in Life sciences -- Chapter 2. Management and Manufacturing process of biologics -- Chapter 3. Downstream processes -- Chapter 4. Bioprinting -- Chapter 5. Biopharmaceuticals: New Frontier.
Record Nr. UNINA-9910424639003321
Behera Basanta Kumara  
Singapore : , : Springer, , [2020]
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Current research in structural biology
Current research in structural biology
Pubbl/distr/stampa [Amsterdam] : , : Elsevier B.V., , 2019-
Descrizione fisica 1 online resource : illustrations
Soggetto topico Molecular dynamics
Macromolecules
Biomolecules
Structure-activity relationships (Biochemistry)
Molecular Biology
Soggetto genere / forma Periodical
Periodicals.
ISSN 2665-928X
Formato Materiale a stampa
Livello bibliografico Periodico
Lingua di pubblicazione eng
Altri titoli varianti CRSB
Structural biology
Record Nr. UNINA-9910384444103321
[Amsterdam] : , : Elsevier B.V., , 2019-
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Current research in structural biology
Current research in structural biology
Pubbl/distr/stampa [Amsterdam] : , : Elsevier B.V., , 2019-
Descrizione fisica 1 online resource : illustrations
Soggetto topico Molecular dynamics
Macromolecules
Biomolecules
Structure-activity relationships (Biochemistry)
Molecular Biology
Soggetto genere / forma Periodical
Periodicals.
ISSN 2665-928X
Formato Materiale a stampa
Livello bibliografico Periodico
Lingua di pubblicazione eng
Altri titoli varianti CRSB
Structural biology
Record Nr. UNISA-996360049103316
[Amsterdam] : , : Elsevier B.V., , 2019-
Materiale a stampa
Lo trovi qui: Univ. di Salerno
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