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Conformational properties of β-residue-containing oligopeptides in apolar solvent

✍ Scribed by Massimiliano Aschi; Adriano Mollica; Gino Lucente; Mario Paglialunga Paradisi; Fernando Mazza

Publisher
Elsevier Science
Year
2006
Tongue
English
Weight
315 KB
Volume
785
Category
Article
ISSN
0022-2860

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Conformations of β-amino acid residues i
Conformations of β-amino acid residues in peptides: X-ray diffraction studies of peptides containing the achiral residue 1-aminocyclohexaneacetic acid, β3,3Ac6c
✍ Prema G. Vasudev; Rajkishor Rai; Narayanaswamy Shamala; Padmanabhan Balaram 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 837 KB

## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides

Erratum: “Conformations of β-amino acid
Erratum: “Conformations of β-amino acid residues in peptides: X-ray diffraction studies of peptides containing the achiral residue 1-aminocyclohexaneacetic acid, β3,3Ac6c”
✍ Prema G. Vasudev; Rajkishor Rai; Narayanaswamy Shamala; Padmanabhan Balaram 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 44 KB 👁 1 views

The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.

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## Abstract The influence of pH upon CD spectra of H‐Trp‐Trp‐OH, H‐Trp‐Trp‐Gly‐OH, and H‐Gly‐Trp‐Trp‐OH is investigated and data are compared with those obtained for peptides containing only one tryptophyl residue. A negative Cotton effect at around 225 nm, which in previous work has been related t