Is polyproline II a major backbone conformation in unfolded proteins?
Top Cited Papers
- 1 January 2002
- book chapter
- Published by Elsevier in Advances in Protein Chemistry
- Vol. 62, 163-240
- https://doi.org/10.1016/s0065-3233(02)62008-x
Abstract
No abstract availableThis publication has 190 references indexed in Scilit:
- Is polyproline II helix the killer conformation? a raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme 1 1Edited by A. R. FershtJournal of Molecular Biology, 2000
- Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)Journal of Molecular Biology, 1998
- Two forms of the pH 4 folding intermediate of apomyoglobinJournal of Molecular Biology, 1998
- Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structuresJournal of Molecular Biology, 1997
- A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein FoldingJournal of Molecular Biology, 1995
- Comparison between the φ Distribution of the Amino Acids in the Protein Database and NMR Data Indicates that Amino Acids have Various φ Propensities in the Random Coil ConformationJournal of Molecular Biology, 1995
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Cold denaturation of myoglobinJournal of Molecular Biology, 1986
- Conformational energy estimates for statistically coiling polypeptide chainsJournal of Molecular Biology, 1967