## Abstract The x‐ray diffraction analyses of three N‐ and C‐terminally blocked L, D dipeptides, namely t‐Boc‐D‐Leu‐L‐Leu‐OMe (1), t‐Boc‐L‐Ile‐D‐alle‐OMe (2), and t‐Boc‐D‐aIle‐L‐Ile‐OMe (3) containing enantiomeric or diastereomeric amino acid residues have been carried out. The structures were dete
Crystal structure and conformation of methionyl dipeptides: Structure ofL-methionyl-L-asparagine: Preferred conformations of peptides containing methionyl and asparaginyl residues
✍ Scribed by Todd Stievater; Thamarapu Srikrishnan
- Book ID
- 106403725
- Publisher
- Springer
- Year
- 2005
- Tongue
- English
- Weight
- 96 KB
- Volume
- 35
- Category
- Article
- ISSN
- 1572-8854
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## Abstract The crystal structure and conformation of the synthetic cyclic tetrapeptide, __cyclo__(L‐Pro‐Sar)~2~, was determined by x‐ray analysis. The peptide crystallizes in the orthorhombic space group __P__2~1~2~1~2~1~ with cell parameters __a__ = 9.277(1), __b__ = 12.884(1), and __c__ = 15.581
The peptide BOC-L-Val-APhe-APhe-L-Val-OCH3 was synthesized by the azlactone method in solution phase, and its crystal and molecular structures were determined by x-ray diffraction method. Single crystals were grown by slow evaporation from a methanol/water solution at 6°C. The crystals belong to an
To obtain general rules of peptide design using alpha, beta-dehydro-residues, a sequence with two consecutive delta Phe-residues, Boc-L-Val-delta Phe-delta Phe-L-Ala-OCH3, was synthesized by azlactone method in solution phase. The peptide was crystallized form its solution in an acetone/water mixtur