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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|
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 | ||
|