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Foldamers [[electronic resource] ] : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by François Diederich
| Foldamers [[electronic resource] ] : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by François Diederich |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2007 |
| Descrizione fisica | 1 online resource (459 p.) |
| Disciplina |
541
547.7 |
| Altri autori (Persone) |
HechtStefan <1974->
HucIvan |
| Soggetto topico |
Chemistry, Technical
Molecules - Models Oligomers |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-281-08796-3
1-282-11841-2 9786612118418 9786611087968 3-527-61147-9 3-527-61148-7 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Foldamers; Foreword; Contents; Preface; List of Contributors; Part 1 Structure: Foldamer Design Concepts; 1 Foldamers Based on Local Conformational Preferences; 1.1 Introduction; 1.2 Rigidly Locked Molecules; 1.3 Predictable Foldamers; 1.3.1 Local Conformational Control; 1.3.2 Folded Conformations of π-conjugated Systems; 1.3.2.1 Crescents and Helices; 1.3.2.2 Linear Strands; 1.3.2.3 Macrocycles; 1.3.3 Partially π-conjugated Oligomers; 1.4 Semi-rigid Backbones; 1.4.1 Tertiary Aromatic Amides, Imides and Ureas; 1.4.2 Tertiary Aliphatic Amides: Polyprolines and Peptoids
1.4.3 Hindered Polymer and Oligomer Backbones1.5 Conformational Transitions; 1.6 Conclusion and Perspectives; References; 2 Foldamers Based on Remote Intrastrand Interactions; 2.1 Introduction; 2.2 What can be Learned from Strategies used to Control Conformations of α-Polypeptides?; 2.3 Helices from Homogeneous Oligomeric Backbones with Periodicity at the Monomer Level: ω-Peptides and their Analogs; 2.3.1 Compact Helices with Large (>10 atoms) H-bonded Rings; 2.3.1.1 The Homologation Strategy: β- and γ-Peptide Foldamers 2.3.1.2 Imposing Backbone Conformational Restriction/Pre-organization for Optimal Helical Folding2.3.1.3 Folding in an Aqueous Environment; 2.3.1.4 Dynamics of β- and γ-Peptide Helices: Evidence for Noncooperative Folding/Unfolding Processes; 2.3.2 Extended Helices with Small H-bonded Rings Centered at a Single Residue; 2.3.2.1 α-Peptides: the γ-Helix; 2.3.2.2 ω-Peptides with Specific Conformation-stabilizing Elements; 2.3.2.3 Stabilizing Local Backbone Conformation by Inverse-Bifurcation Involving an Additional Heteroatom; 2.4 Oligoamide Mixed Helices 2.4.1 The α-Oligopeptide Precedent: from Antibiotic Gramicidin A to Poly-Gln Aggregates in Huntington's Disease2.4.2 Introducing Periodicity at the Level of a Dimer Unit in β-Peptides leads to a Remarkably Stable Mixed Helical Fold; 2.4.2.1 By Mixing β(2)- and β(3)-Amino Acids; 2.4.2.2 Additional Substitution Patterns Stabilizing the Mixed 10/12- (12/10-) Helix; 2.4.3 Extending the Concept of Mixed Helices; 2.5 Nonperiodic Structures: Open Chain β-Turn-like Motifs and Hairpins in Designed Homo-oligomers; 2.5.1 Sheet-forming ω-peptides; 2.5.2 Turn Segment for Hairpin Formation 2.6 Expanding Structural Diversity with Heterogeneous Backbones2.6.1 From Discrete ω-Amino Acid Guests in α-Helices to Helical α,ω- and β,γ-Peptide Hybrids; 2.6.2 Hairpins from α,ω-Peptide Hybrids; 2.6.3 Sculpting New Shapes by Integrating H-Bonding, Aromatic Interactions and Multiple Levels of Pre-organization; 2.7 Conclusion and Outlook; References; 3 Foldamers Based on Solvophobic Effects; 3.1 Introduction; 3.2 Learning from Solvophobically Driven Assemblies - Intermolecular Solvophobic Interactions; 3.3 Learning from Synthetic and Biological Polymers 3.4 Recent Advances in Foldamers Based on Solvophobic Effects |
| Record Nr. | UNINA-9910144010903321 |
| Weinheim, : Wiley-VCH, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Foldamers [[electronic resource] ] : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by François Diederich
| Foldamers [[electronic resource] ] : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by François Diederich |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2007 |
| Descrizione fisica | 1 online resource (459 p.) |
| Disciplina |
541
547.7 |
| Altri autori (Persone) |
HechtStefan <1974->
HucIvan |
| Soggetto topico |
Chemistry, Technical
Molecules - Models Oligomers |
| ISBN |
1-281-08796-3
1-282-11841-2 9786612118418 9786611087968 3-527-61147-9 3-527-61148-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Foldamers; Foreword; Contents; Preface; List of Contributors; Part 1 Structure: Foldamer Design Concepts; 1 Foldamers Based on Local Conformational Preferences; 1.1 Introduction; 1.2 Rigidly Locked Molecules; 1.3 Predictable Foldamers; 1.3.1 Local Conformational Control; 1.3.2 Folded Conformations of π-conjugated Systems; 1.3.2.1 Crescents and Helices; 1.3.2.2 Linear Strands; 1.3.2.3 Macrocycles; 1.3.3 Partially π-conjugated Oligomers; 1.4 Semi-rigid Backbones; 1.4.1 Tertiary Aromatic Amides, Imides and Ureas; 1.4.2 Tertiary Aliphatic Amides: Polyprolines and Peptoids
1.4.3 Hindered Polymer and Oligomer Backbones1.5 Conformational Transitions; 1.6 Conclusion and Perspectives; References; 2 Foldamers Based on Remote Intrastrand Interactions; 2.1 Introduction; 2.2 What can be Learned from Strategies used to Control Conformations of α-Polypeptides?; 2.3 Helices from Homogeneous Oligomeric Backbones with Periodicity at the Monomer Level: ω-Peptides and their Analogs; 2.3.1 Compact Helices with Large (>10 atoms) H-bonded Rings; 2.3.1.1 The Homologation Strategy: β- and γ-Peptide Foldamers 2.3.1.2 Imposing Backbone Conformational Restriction/Pre-organization for Optimal Helical Folding2.3.1.3 Folding in an Aqueous Environment; 2.3.1.4 Dynamics of β- and γ-Peptide Helices: Evidence for Noncooperative Folding/Unfolding Processes; 2.3.2 Extended Helices with Small H-bonded Rings Centered at a Single Residue; 2.3.2.1 α-Peptides: the γ-Helix; 2.3.2.2 ω-Peptides with Specific Conformation-stabilizing Elements; 2.3.2.3 Stabilizing Local Backbone Conformation by Inverse-Bifurcation Involving an Additional Heteroatom; 2.4 Oligoamide Mixed Helices 2.4.1 The α-Oligopeptide Precedent: from Antibiotic Gramicidin A to Poly-Gln Aggregates in Huntington's Disease2.4.2 Introducing Periodicity at the Level of a Dimer Unit in β-Peptides leads to a Remarkably Stable Mixed Helical Fold; 2.4.2.1 By Mixing β(2)- and β(3)-Amino Acids; 2.4.2.2 Additional Substitution Patterns Stabilizing the Mixed 10/12- (12/10-) Helix; 2.4.3 Extending the Concept of Mixed Helices; 2.5 Nonperiodic Structures: Open Chain β-Turn-like Motifs and Hairpins in Designed Homo-oligomers; 2.5.1 Sheet-forming ω-peptides; 2.5.2 Turn Segment for Hairpin Formation 2.6 Expanding Structural Diversity with Heterogeneous Backbones2.6.1 From Discrete ω-Amino Acid Guests in α-Helices to Helical α,ω- and β,γ-Peptide Hybrids; 2.6.2 Hairpins from α,ω-Peptide Hybrids; 2.6.3 Sculpting New Shapes by Integrating H-Bonding, Aromatic Interactions and Multiple Levels of Pre-organization; 2.7 Conclusion and Outlook; References; 3 Foldamers Based on Solvophobic Effects; 3.1 Introduction; 3.2 Learning from Solvophobically Driven Assemblies - Intermolecular Solvophobic Interactions; 3.3 Learning from Synthetic and Biological Polymers 3.4 Recent Advances in Foldamers Based on Solvophobic Effects |
| Record Nr. | UNINA-9910830554803321 |
| Weinheim, : Wiley-VCH, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Foldamers : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by Francois Diederich
| Foldamers : structure, properties, and applications / / edited by Stefan Hecht and Ivan Huc ; foreword by Francois Diederich |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2007 |
| Descrizione fisica | 1 online resource (459 p.) |
| Disciplina |
541
547.7 |
| Altri autori (Persone) |
HechtStefan <1974->
HucIvan |
| Soggetto topico |
Chemistry, Technical
Molecules - Models Oligomers |
| ISBN |
1-281-08796-3
1-282-11841-2 9786612118418 9786611087968 3-527-61147-9 3-527-61148-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Foldamers; Foreword; Contents; Preface; List of Contributors; Part 1 Structure: Foldamer Design Concepts; 1 Foldamers Based on Local Conformational Preferences; 1.1 Introduction; 1.2 Rigidly Locked Molecules; 1.3 Predictable Foldamers; 1.3.1 Local Conformational Control; 1.3.2 Folded Conformations of π-conjugated Systems; 1.3.2.1 Crescents and Helices; 1.3.2.2 Linear Strands; 1.3.2.3 Macrocycles; 1.3.3 Partially π-conjugated Oligomers; 1.4 Semi-rigid Backbones; 1.4.1 Tertiary Aromatic Amides, Imides and Ureas; 1.4.2 Tertiary Aliphatic Amides: Polyprolines and Peptoids
1.4.3 Hindered Polymer and Oligomer Backbones1.5 Conformational Transitions; 1.6 Conclusion and Perspectives; References; 2 Foldamers Based on Remote Intrastrand Interactions; 2.1 Introduction; 2.2 What can be Learned from Strategies used to Control Conformations of α-Polypeptides?; 2.3 Helices from Homogeneous Oligomeric Backbones with Periodicity at the Monomer Level: ω-Peptides and their Analogs; 2.3.1 Compact Helices with Large (>10 atoms) H-bonded Rings; 2.3.1.1 The Homologation Strategy: β- and γ-Peptide Foldamers 2.3.1.2 Imposing Backbone Conformational Restriction/Pre-organization for Optimal Helical Folding2.3.1.3 Folding in an Aqueous Environment; 2.3.1.4 Dynamics of β- and γ-Peptide Helices: Evidence for Noncooperative Folding/Unfolding Processes; 2.3.2 Extended Helices with Small H-bonded Rings Centered at a Single Residue; 2.3.2.1 α-Peptides: the γ-Helix; 2.3.2.2 ω-Peptides with Specific Conformation-stabilizing Elements; 2.3.2.3 Stabilizing Local Backbone Conformation by Inverse-Bifurcation Involving an Additional Heteroatom; 2.4 Oligoamide Mixed Helices 2.4.1 The α-Oligopeptide Precedent: from Antibiotic Gramicidin A to Poly-Gln Aggregates in Huntington's Disease2.4.2 Introducing Periodicity at the Level of a Dimer Unit in β-Peptides leads to a Remarkably Stable Mixed Helical Fold; 2.4.2.1 By Mixing β(2)- and β(3)-Amino Acids; 2.4.2.2 Additional Substitution Patterns Stabilizing the Mixed 10/12- (12/10-) Helix; 2.4.3 Extending the Concept of Mixed Helices; 2.5 Nonperiodic Structures: Open Chain β-Turn-like Motifs and Hairpins in Designed Homo-oligomers; 2.5.1 Sheet-forming ω-peptides; 2.5.2 Turn Segment for Hairpin Formation 2.6 Expanding Structural Diversity with Heterogeneous Backbones2.6.1 From Discrete ω-Amino Acid Guests in α-Helices to Helical α,ω- and β,γ-Peptide Hybrids; 2.6.2 Hairpins from α,ω-Peptide Hybrids; 2.6.3 Sculpting New Shapes by Integrating H-Bonding, Aromatic Interactions and Multiple Levels of Pre-organization; 2.7 Conclusion and Outlook; References; 3 Foldamers Based on Solvophobic Effects; 3.1 Introduction; 3.2 Learning from Solvophobically Driven Assemblies - Intermolecular Solvophobic Interactions; 3.3 Learning from Synthetic and Biological Polymers 3.4 Recent Advances in Foldamers Based on Solvophobic Effects |
| Record Nr. | UNINA-9910877205803321 |
| Weinheim, : Wiley-VCH, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||