Structure of the 3101-helical pentapeptide Boc-l-Pro-Aib-l-Ala-Aib-l-Ala-OH
โ Scribed by Bosch, R. ;Jung, G. ;Schmitt, H. ;Winter, W.
- Book ID
- 114503291
- Publisher
- International Union of Crystallography
- Year
- 1985
- Tongue
- English
- Weight
- 593 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0108-2701
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๐ SIMILAR VOLUMES
## Abstract The xโray structure of BocโLโAlaโAibโAlaโAibโAlaโGlu(OBzl)โAlaโAibโAlaโAibโAlaโOMe(I) represents the first ฮฑโhelix determined by direct methods. This undecapeptide is a model of the Nโterminus of alamethicin, and it exhibits voltageโdependent pores in bilayer membranes at a higher volta
## Synopsis t -Butyloxycarbonyl-~-alanyl-a-aminoisobutyryl-~-alanyl-a-aminoisobutyryl-a-aminoisobutyric acid methyl ester ( t -Boc-L-Ala-Aib-L-Ala-Aib-Aib-OMe), C24H43N508, an end-protected pentapeptide with a sequence corresponding to the 6th through the 10th residues in suzukacillin, crystallize
## Synopsis A second example of insertion of a water molecule into the helical backbone of an apolar peptide is presented here and compared to a similar occurrence in a longer peptide with the same type of sequence of residues, i.e., Boc-Aib-(Ala-Leu-fib),-OMe. The backbone of the title compound a