Glu-Ala-Ala-Glu-Lys-Ala
Conformational Study in Water by NMR and Molecular Modeling of α-Methyl-α-Amino Acid: Differential Conformational Properties of α-Cyclic and α-Methylglutamic Acid
✍ Scribed by Todeschi, N.; Gharbi-Benarous, J.; Arulmozhi, V.; Acher, F.; Azerad, R.; Girault, J.-P.
- Book ID
- 127252230
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 289 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0095-2338
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A series of terminally blocked peptides (to the pentamer level) from L-Ala and the cyclic C h,h -disubstituted Gly residue Afc and one Gly/Afc dipeptide have been synthesized by solution method and fully characterized. The molecular structure of the amino acid derivative Boc-Afc-OMe and the dipeptid
## Abstract C^α^‐Tetrasubstituted α‐amino acids are widely used to design and prepare peptides and peptide mimics with constrained conformations. Subcategories of these compounds are cyclic C^α^‐tetrasubstituted α‐amino acids, in which both α‐substituents are covalently connected. This survey prese
## Abstract The validity of Silberberg's hypothesis concerning the conformation of branched polypeptides was tested by studies on solutions and on monolayers. The poly(α‐amino acids) investigated consisted of poly‐L‐lysine backbones with side chains of poly(gamma;‐benzyl L‐gutamate) and poly(β‐benz