Truncated staphylococcal nuclease is compact but disordered.
- 15 January 1992
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 89 (2), 748-752
- https://doi.org/10.1073/pnas.89.2.748
Abstract
Deletion of 13 amino acids from the carboxyl terminus of the 149-amino acid staphylococcal nuclease molecule results in a denatured, partly unfolded molecule that lacks persistent secondary structure but is compact under physiological conditions. Since the modification is a carboxyl-terminal deletion, it is argued that the state resembles a peptide emerging from the ribosome just before the complete folding pathway is initiated. In this paper, we characterize the molecule by nuclear magnetic resonance, circular dichroism, and small-angle x-ray scattering measurements. The truncated nuclease shows wild-type levels of activity in the presence of calcium and is found to fold into a native-like conformation in the presence of 3',5'-bisphospho-2'-deoxythymidine, a potent inhibitor. Thus, the truncated molecule retains the capacity to fold. Our results suggest that extensive solvent exclusion generates a compact polypeptide chain prior to the development of persistent secondary structural features as a protein folds during biosynthesis.Keywords
This publication has 28 references indexed in Scilit:
- Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMRBiochemistry, 1990
- Dominant forces in protein foldingBiochemistry, 1990
- Coupling between local structure and global stability of a protein: mutants of staphylococcal nucleaseBiochemistry, 1990
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nucleaseBiochemistry, 1989
- Comparison of the crystal and solution structures of calmodulin and troponin CBiochemistry, 1988
- The efficiency of folding of some proteins is increased by controlled rates of translation in vivoJournal of Molecular Biology, 1987
- Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle x-ray scatteringBiochemistry, 1985
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981