Relationship between α-helical propensity and formation of the ribonuclease-S complex
- 15 July 1975
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 95 (4), 497-511
- https://doi.org/10.1016/0022-2836(75)90313-7
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Analysis of Conformations of Amino Acid Residues and Prediction of Backbone Topography in ProteinsIsrael Journal of Chemistry, 1974
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Evolution of Ribonuclease in Relation to Polypeptide Folding MechanismsNature, 1972
- Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. VI. Leucine Parameters from Random Poly(hydroxypropylglutamine-co-L-leucine) and Poly(hydroxybutylglutamine-co-L-leucine)Macromolecules, 1972
- Conformational Analysis of Biopolymers: Conformational Energy CalculationsAnnual Review of Biophysics and Bioengineering, 1972
- Thermodynamic parameters of helix‐coil transition in polypeptide chains I. Poly‐(L‐glutamic acid)Biopolymers, 1971
- Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. III. Glycine Parameters from Random Poly(hydroxybutylglutamine-co-glycine)Macromolecules, 1971
- Helix-coil transition of the isolated amino terminus of ribonucleaseBiochemistry, 1971
- Extent and stability of the α‐helix in γ‐benzyl L‐glutamate–glycine copolymersBiopolymers, 1967
- THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION1,2Journal of the American Chemical Society, 1960