prolyl-serine has been researched along with seryl-proline* in 1 studies
1 other study(ies) available for prolyl-serine and seryl-proline
| Article | Year |
|---|---|
Incorporation of Ahc into model dipeptides as an inducer of a beta-turn with a distorted amide bond. Conformational analysis.
The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides. The conformational analysis of the new peptides in the solid state revealed that the Ahc-Ser sequence displays a type I beta-turn, which includes a distorted amide bond. In contrast, the Ser-Ahc sequence exists in a nonfolded structure. Topics: Bridged Bicyclo Compounds, Heterocyclic; Carboxylic Acids; Catalysis; Chromatography, Thin Layer; Dipeptides; Esters; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Proline; Protein Structure, Secondary; Serine; X-Ray Diffraction | 2002 |