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Structure of the 310-helical pentapeptide Boc-Aib-l-Ala-Aib-l-Ala-Aib-OMe dihydrate, C24H43N5O8.2H2O

โœ Scribed by Bosch, R. ;Jung, G. ;Winter, W.


Book ID
114501497
Publisher
International Union of Crystallography
Year
1983
Tongue
English
Weight
319 KB
Volume
39
Category
Article
ISSN
0108-2701

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Crystal structure of the ฮฑ-helical undec
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## Abstract The xโ€ray structure of Bocโ€Lโ€Alaโ€Aibโ€Alaโ€Aibโ€Alaโ€Glu(OBzl)โ€Alaโ€Aibโ€Alaโ€Aibโ€Alaโ€OMe(I) represents the first ฮฑโ€helix determined by direct methods. This undecapeptide is a model of the Nโ€terminus of alamethicin, and it exhibits voltageโ€dependent pores in bilayer membranes at a higher volta

Solvated helical backbones: X-ray diffra
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## 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

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## 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