Cookies helfen uns bei der Bereitstellung unserer Dienste. Durch die Nutzung unserer Dienste erklären Sie sich damit einverstanden, dass wir Cookies setzen.

Cuvillier Verlag

30 Jahre Kompetenz im wissenschaftlichen Publizieren
Internationaler Fachverlag für Wissenschaft und Wirtschaft

Cuvillier Verlag

De En Es
Extending the scope of protein synthesis by a novel auxiliary‐based Native Chemical Ligation strategy

Printausgabe
EUR 35,30 EUR 33,54

E-Book
EUR 24,71

Extending the scope of protein synthesis by a novel auxiliary‐based Native Chemical Ligation strategy

Christina Nadler (Autor)

Vorschau

Leseprobe, PDF (480 KB)
Inhaltsverzeichnis, PDF (56 KB)

ISBN-13 (Printausgabe) 9783954045044
ISBN-13 (E-Book) 9783736945043
Sprache Englisch
Seitenanzahl 198
Umschlagkaschierung matt
Auflage 1. Aufl.
Erscheinungsort Göttingen
Promotionsort Göttingen
Erscheinungsdatum 18.09.2013
Allgemeine Einordnung Dissertation
Fachbereiche Chemie
Organische Chemie
Schlagwörter Organische Chemie, Peptidchemie, Festphasensynthese, SPPS, Native Chemical Ligation, cystein-freie Native Chemical Ligation, Ligationsauxiliar, Photolabilität, artifizielle Aminosäuren, Histidinmimetika, Single Amino Acid Chelate, Kupfer-katalysierte Azid-Alkin-Cycloaddition, Fluoreszenzspektroskopie, Zinksensoren, Zinkfingerpeptide, Zif268, Substratanalogon, Lipoxygenase.
Beschreibung

There is a constant need for developing improved methods for introducing artificial functionalities into peptides and proteins, as the modification of peptides and proteins is one of the major routes to investigate biological function in vitro and in vivo, e.g. by introduction of spin labels or fluorophores. To improve the synthetic accessibility of chemically modified peptides and proteins a new cysteine-free Native Chemical Ligation strategy based on a photocleavable auxiliary was developed and successfully implemented. In addition, a novel protocol for labeling peptides and proteins by introducing artificial, histidine-mimicking amino acids was devised. These triazole-based building blocks were utilized for the introduction of additional metal binding sites into peptides as well as for the development of peptidic zinc sensors based on zinc finger peptide Zif268.