Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.
- 1 October 1996
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (20) , 10703-10706
- https://doi.org/10.1073/pnas.93.20.10703
Abstract
Fibronectin type III modules contain approximately 90 residues and are an extremely common building block of animal proteins. Despite containing a complex all-beta-sheet topology and eight prolines, the refolding of the 10th type III module of human fibronectin has been found to be very rapid, with native core packing, amide hydrogen bonding, and backbone conformation all recovered within 1 s at 5 degrees C. These observations indicate that this domain can overcome many structural characteristics often thought to slow the folding process.Keywords
This publication has 29 references indexed in Scilit:
- Extremely rapid protein folding in the absence of intermediatesNature Structural & Molecular Biology, 1995
- Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy.Proceedings of the National Academy of Sciences, 1989
- A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nucleaseBiochemistry, 1989
- Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chainJournal of Molecular Biology, 1982
- Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand.The Journal of cell biology, 1981
- A Native‐Like Intermediate on the Ribonuclease A Folding PathwayEuropean Journal of Biochemistry, 1981
- A Native‐Like Intermediate on the Ribonuclease A Folding PathwayEuropean Journal of Biochemistry, 1981
- Effect of proline residues on protein foldingJournal of Molecular Biology, 1981
- Role of proline isomerization in folding of ribonuclease A at low temperaturesProceedings of the National Academy of Sciences, 1979
- Possible implications of many proline residues for the kinetics of protein unfolding and refoldingJournal of Molecular Biology, 1978