[2] Modified amino acids as probes of helix stability
- 1 January 1998
- book chapter
- Published by Elsevier
- Vol. 295, 26-41
- https://doi.org/10.1016/s0076-6879(98)95033-9
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Distinguishing Helix Conformations in Alanine-Rich Peptides Using the Unnatural Amino Acid TOAC and Electron Spin ResonanceJournal of the American Chemical Society, 1996
- Guidelines for Protein Design: The Energetics of β Sheet Side Chain InteractionsScience, 1995
- LINUS: A hierarchic procedure to predict the fold of a proteinProteins-Structure Function and Bioinformatics, 1995
- Helix-Forming Tendencies of Amino Acids in Short (Hydroxybutyl)-L-glutamine Peptides: An Evaluation of the Contradictory Results from Host-Guest Studies and Short Alanine-Based PeptidesBiochemistry, 1994
- Elucidating the folding problem of helical peptides using empirical parametersNature Structural & Molecular Biology, 1994
- Measurement of the β-sheet-forming propensities of amino acidsNature, 1994
- Amino Acid Preferences for Specific Locations at the Ends of α HelicesScience, 1988
- Helix Signals in ProteinsScience, 1988
- The role of the α-helix dipole in protein function and structureProgress in Biophysics and Molecular Biology, 1985
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974