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

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

Christina Nadler (Autor)

Previo

Lectura de prueba, PDF (480 KB)
Indice, PDF (56 KB)

ISBN-13 (Impresion) 9783954045044
ISBN-13 (E-Book) 9783736945043
Idioma Inglés
Numero de paginas 198
Laminacion de la cubierta mate
Edicion 1. Aufl.
Lugar de publicacion Göttingen
Lugar de la disertacion Göttingen
Fecha de publicacion 18.09.2013
Clasificacion simple Tesis doctoral
Area Química
Química orgánica
Palabras claves 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.
Descripcion

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.