## Abstract The conformational features of a peptide derived by the 10β30 sequence of the mitochondrial domain of AKAP121 [Acβ^1^XKKPLALPGMLALLGWWWFFSRKKX^25^βNH~2~ (X = Ξ²βAla)] in water and in a water/triflouroethanol (TFE) mixture at 298 K have been determined by NMR and CD spectroscopy. Backbone
A Synthetic Receptor Motif Designed for Extended Peptide Conformations
β Scribed by Kevin Ryan; Leland J Gershell; W Clark Still
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- French
- Weight
- 166 KB
- Volume
- 56
- Category
- Article
- ISSN
- 0040-4020
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## Abstract Peptide models have been widely used to investigate conformational aspects of domains of proteins since the early 1950s. A pioneer in this field was Dr. Murray Goodman, who applied a battery of methodologies to study the onset of structure in homooligopeptides. This article reviews some
Background The serpin-enzyme complex receptor (SECR) has previously been successfully targeted for gene delivery using synthetic peptide ligands covalently linked in fluid phase to commercially available polylysine preparations (y10-54 kDa). The objective of the present study was to improve this app