The architectures (three-dimensional shapes) of peptides determine their respective biological functions. Therefore, the correct alignment of functionalities in a structure by constraining the flexibility is a key process in evolution as well as in medicinal chemistry in order to increase binding affinity and selectivity. The rigidification of a peptide chain can have local effects (incorporation of the amino acid proline) or it can globally restrain flexibility (macrocyclization). Furthermore, the combination of both strategies has given rise to complex antibiotics with highly optimized modes of action. This work approaches these principles in three topics and for different purposes. The first chapter presents a novel scanning strategy which utilizes synthetic local rigidifications for the evaluation of Neuropeptide Y structure and receptor binding patterns. The fundamental process of macrocyclization is topic of the second chapter. For iminopeptides, ring-chain equilibria can be established and controlled, thereby allowing for the thermodynamic analysis of the ring closure. This leads to the identification of structural determinants that influence the inclination of a peptide chain to close the ring. In the third chapter, a sugarbased synthetic pathway leading to highly functionalized thiazole dipeptides is described. This strategy led to the synthesis of core motivs of complex thiopeptide antibiotics, as well as to diastereomers and homologs thereof.
Sebastian Pape discusses two different scenarios for authentication. On the one hand, users cannot trust their devices and nevertheless want to be able to do secure authentication. On the other hand, users may not want to be tracked while their service provider does not want them to share their credentials. Many users may not be able to determine whether their device is trustworthy, i.e. it might contain malware. One solution is to use visual cryptography for authentication. The author generalizes this concept to human decipherable encryption schemes and establishes a relationship to CAPTCHAS. He proposes a new security model and presents the first visual encryption scheme which makes use of noise to complicate the adversary's task. To prevent service providers from keeping their users under surveillance, anonymous credentials may be used. However, sometimes it is desirable to prevent the users from sharing their credentials. The author compares existing approaches based on non-transferable anonymous credentials and proposes an approach which combines biometrics and smartcards.
This book provides a comprehensive overview of stacking faults in crystal structures. Subjects covered include: notations used in representations of close-packed structures; types of faults; methods of detection and measurement such as X-ray diffraction, electron diffraction and other techniques; theoretical models of non-random faulting during phase transitions; specific examples of - close packed structures including, zinc sulphide, silicon carbide and silver iodide.
The architectures (three-dimensional shapes) of peptides determine their respective biological functions. Therefore, the correct alignment of functionalities in a structure by constraining the flexibility is a key process in evolution as well as in medicinal chemistry in order to increase binding affinity and selectivity. The rigidification of a peptide chain can have local effects (incorporation of the amino acid proline) or it can globally restrain flexibility (macrocyclization). Furthermore, the combination of both strategies has given rise to complex antibiotics with highly optimized modes of action. This work approaches these principles in three topics and for different purposes. The first chapter presents a novel scanning strategy which utilizes synthetic local rigidifications for the evaluation of Neuropeptide Y structure and receptor binding patterns. The fundamental process of macrocyclization is topic of the second chapter. For iminopeptides, ring-chain equilibria can be established and controlled, thereby allowing for the thermodynamic analysis of the ring closure. This leads to the identification of structural determinants that influence the inclination of a peptide chain to close the ring. In the third chapter, a sugarbased synthetic pathway leading to highly functionalized thiazole dipeptides is described. This strategy led to the synthesis of core motivs of complex thiopeptide antibiotics, as well as to diastereomers and homologs thereof.
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