A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state
- 1 December 1992
- journal article
- letter
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 114 (25) , 10079-10081
- https://doi.org/10.1021/ja00051a061
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- A tetrahedral zinc(II)-binding site introduced into a designed proteinBiochemistry, 1990
- De Novo Design, Expression, and Characterization of Felix: a Four-Helix Bundle Protein of Native-Like SequenceScience, 1990
- Design and Synthesis of a Peptide Having Chymotrypsin-Like Esterase ActivityScience, 1990
- Synthesis and biophysical characterization of engineered topographic immunogenic determinants with .alpha..alpha. topologyBiochemistry, 1990
- Synthesis, purification and initial structural characterization of octarellin, a de novo polypeptide modelled on the α/β-barrel ProteinsProtein Engineering, Design and Selection, 1990
- Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbuminBiochemistry, 1989
- Characterization of a Helical Protein Designed from First PrinciplesScience, 1988
- Analysis of the relationship between side-chain conformation and secondary structure in globular proteinsJournal of Molecular Biology, 1987
- The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins.Journal of Biological Chemistry, 1986
- Three-state denaturation of α-lactalbumin by guanidine hydrochlorideJournal of Molecular Biology, 1976