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Studies on the conformation of amino acids VII. Backbone and side-chain conformations of N-terminal residues in peptides

✍ Scribed by P.K. Ponnuswamy; V. Sasisekharan


Book ID
115748688
Publisher
Elsevier Science
Year
1970
Weight
318 KB
Volume
221
Category
Article
ISSN
0005-2795

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πŸ“œ SIMILAR VOLUMES


Backbone and side-chain conformations of
✍ 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

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Semiempirical AM1 calculations were carried out for quantum-chemically optimized minimum energy conformations of peptides (Ala) 4 -X-(Ala) 4 , where X stands for different L-␣amino acids (Ala,

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✍ F. Maser; B. Klein; M. Mutter; C. Toniolo; G. M. Bonora πŸ“‚ Article πŸ“… 1983 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 302 KB πŸ‘ 2 views

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-

Residual Dipolar Couplings in Short Pept
✍ Markus B. Schmid; Matthias Fleischmann; Valerio D'Elia; Oliver Reiser; Wolfram G πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 520 KB

## Abstract **A flexible tool for rigid systems**. Residual dipolar couplings (RDCs) have proven to be valuable NMR structural parameters that provide insights into the backbone conformations of short linear peptidic foldamers, as illustrated here. This study demonstrates that RDCs at natural abund