Conformation and crystal structure of the cyclic polypeptide [Gly-Gly-D-Ala-D-Ala-Gly-Gly] .3H2O
β Scribed by Karle, Isabella L.; Gibson, J. W.; Karle, Jerome.
- Book ID
- 126509702
- Publisher
- American Chemical Society
- Year
- 1970
- Tongue
- English
- Weight
- 513 KB
- Volume
- 92
- Category
- Article
- ISSN
- 0002-7863
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π SIMILAR VOLUMES
The molecular and crystal structure of one of the crystalline modifications of Bombyx mori, silk I, was determined by x-ray diffraction method. Cell dimensions are essentially the same as those found in the synthetic model peptide poly(L-Ala-Gly). The (, ) values of L-Ala and Gly in the repeating un
## Synopsis Conformational analysis of triple helices of a type of collagen was performed with typical collagen tripeptide sequences based on Gly-Pro-Ala, Gly-Ala-Hyp, and Gly-Ala-Ala. During energy minimization, the possibility of continual deformation of the pyrrolidine cycle was taken into acco