Synthesis of α-helix-forming peptides by gene engineering methods and their characterization by circular dichroism spectra measurements
- 1 May 1996
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1294 (2) , 129-137
- https://doi.org/10.1016/0167-4838(96)00003-9
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- The energetics of ion-pair and hydrogen-bonding interactions in a helical peptideBiochemistry, 1993
- A single-stranded amphipathic .alpha.-helix in aqueous solution: Design, structural characterization, and its application for determining .alpha.-helical propensities of amino acidsBiochemistry, 1993
- Packing and hydrophobicity effects on protein folding and stability: Effects of β‐branched amino acids, valine and isoleucine, on the formation and stability of two‐stranded α‐helical coiled coils/leucine zippersProtein Science, 1993
- Large differences in the helix propensities of alanine and glycineNature, 1991
- A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino AcidsScience, 1990
- Side Chain Contributions to the Stability of Alpha-Helical Structure in PeptidesScience, 1990
- Relative helix-forming tendencies of nonpolar amino acidsNature, 1990
- On the Theory of Helix—Coil Transition in PolypeptidesThe Journal of Chemical Physics, 1961
- Theory of the Phase Transition between Helix and Random Coil in Polypeptide ChainsThe Journal of Chemical Physics, 1959