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
Modeling of the Amino Acid Side Chain Effects on Peptide Conformation
✍ Scribed by Katrin Sak; Mati Karelson; Jaak Järv
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 76 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0045-2068
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✦ Synopsis
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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## Abstract Understanding the hydrophilicity/hydrophobicity of amino acid side chains in peptides/proteins is one the most important aspects of biology. Though many hydrophilicity/hydrophobicity scales have been generated, an “intrinsic” scale has yet to be achieved. “Intrinsic” implies the maximum