𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Conformational preferences of side-chain protected amino acid residues and their impact in peptide synthesis

✍ Scribed by F. Maser; B. Klein; M. Mutter; C. Toniolo; G. M. Bonora

Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
302 KB
Volume
22
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

Using the host-guest technique, tentative scales for the helix-inducing power and the (3-structure-forming potential of various side-chain protected amino acid residues in trifluoroethanol are established mainly by CD measurements. The generally lower tendency for (3-structure formation of the host-guest peptides compared to that of the host peptide is discussed. The influence of these conformational features on the solubility of the peptides is also pointed out.

πŸ“œ SIMILAR VOLUMES

Backbone and side-chain conformations of
Backbone and side-chain conformations of amino acids and amino acid residues in peptides
✍ V. Sasisekharan; P. K. Ponnuswamy πŸ“‚ Article πŸ“… 1970 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 198 KB πŸ‘ 2 views

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

Effect of phenyl ring position in the CΞ±
Effect of phenyl ring position in the CΞ±-methylated Ξ±-amino acid side chain on peptide preferred conformation
✍ C. Toniolo; M. Crisma; F. Formaggio; A. Polese; M. Doi; T. Ishida; E. Mossel; Q. πŸ“‚ Article πŸ“… 1996 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 308 KB πŸ‘ 1 views

The preferred conformations of C"-methyl phenylglycine, C"-methyl phenylalanine, and C"-methyl homophenylalanine residues, as determined in model peptides (including homopeptides) by Fourier transform ir absorption, 'H-nmr, CD, and x-ray diffraction techniques, are compared with the aim of investiga

Partial molar volumes of the amino acid
Partial molar volumes of the amino acid side-chains of proteins in aqueous solution: Some comments on their estimation using partial molar volumes of amino acids and small peptides
✍ Gavin R. Hedwig πŸ“‚ Article πŸ“… 1992 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 317 KB πŸ‘ 2 views

using partial molar volume data, V t , in aqueous solution at 25Β°C for some peptides of sequence Gly-X-Gly, where X is an amino acid. These side-chain partial molar volumes are critically compared with those obtained using V data for amino acids. It is concluded that side-chain partial molar volumes