The Helix-Destabilizing Propensity Scale ofd-Amino Acids: The Influence of Side Chain Steric Effects
- 1 May 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (20), 4865-4870
- https://doi.org/10.1021/ja9940524
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Monitoring of α-helical secondary structures in peptides by reversed-phase HPLC of replacement setsAnalytica Chimica Acta, 1997
- d-AMINO ACIDS IN ANIMAL PEPTIDESAnnual Review of Biochemistry, 1997
- Conformational and Functional Study of Magainin 2 in Model Membrane Environments Using the New Approach of Systematic Double-d-Amino Acid ReplacementBiochemistry, 1996
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- The presence of free D-aspartic acid in rodents and manBiochemical and Biophysical Research Communications, 1986
- Influence of temperature on the intrinsic viscosities of proteins in random coil conformationBiochemistry, 1974