Solid-state and solution conformation of N-tert-butyloxycarbonyl-L-prolylglycine.
The occurrence of the oxy analogue in the trans-II 4 leads to 1 intramolecularly hydrogen-bonded nonhelical peptide conformation, recently proposed for t-BOC-L-Pro-Gly-OH in the solid state on the basis of infrared absorption evidence, has been disproved by x-ray diffraction analysis. This type of folding is also absent in polar solvents. However, in solvents of low polarity the presence of this folded form cannot be excluded.
D002942:Circular Dichroism; D005998:Glycine; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides; D011392:Proline; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013816:Thermodynamics; D014961:X-Ray Diffraction
D010455:Peptides; D011392:Proline; D005998:Glycine