Designed Amino Acids That Induce β-Sheet Folding and β-Sheet Interactions in Peptides
✍ Scribed by James S. Nowick; Kit S. Lam; Chris M. Gothard; Jeffrey K. Huon; William E. Kemnitzer; Tatyana Khasanova; Hong Woo Kim; Ruiwu Liu; Santanu Maitra; Hao T. Mee; et al. et al.
- Publisher
- John Wiley and Sons
- Year
- 2003
- Weight
- 57 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0931-7597
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📜 SIMILAR VOLUMES
Folding type-specific secondary structure propensities of 20 naturally occurring amino acids have been derived from a-helical, b-sheet, a/b, and a/b proteins of known structures. These data show that each residue type of amino acids has intrinsic propensities in different regions of secondary struct
The dehydro-residue containing peptides N-Ac-dehydro-Phe-L-Leu-OCH3 ( I ) and N-Acdehydro-Phe-NorVal-OCH, (11) were synthesized by the usual workup procedures. The peptides crystallize from their solutions in methanol in space group P6,: ( I ) a = b = 12.528(2) A, c = 21.653(5) A; (11) a = b = 12.53