The complex multiplet proton NMR pattern at 360 MHz of the propionic side chains in methyl pheophorbides and a pheofarnesin derived from bacteriochZorophyZl-d is capletely analyzed; the major preferred orientation in solution is found to be different from that determined by single crystal X-ray stud
Side-chain and ring D conformation in cholanic acids
โ Scribed by Giglio, E. ;Quagliata, C.
- Book ID
- 117859394
- Publisher
- International Union of Crystallography
- Year
- 1975
- Weight
- 422 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0567-7408
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๐ SIMILAR VOLUMES
The conformational freedom of amino acid side chains is strongly reduced when the side chains occur on an a-helix. A quantitative evaluation of this freedom has been carried out by means of conformational energy computations for all naturally occurring amino acids and for a-aminobutyric acid when th
Although the conformations of two linked peptide units both with glycyl and alanyl residues have been extensively studied,'-$ no systematic investigation of the energies of conformations of two linked peptide units with side chains beyond the CB atom and a comparison with the available crystallograp