Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus.
A 130-residue fragment (D1-D4) taken from a fibronectin-binding protein of Staphylococcus aureus, which contains four fibronectin-binding repeats and is unfolded but biologically active at neutral pH, has been studied extensively by NMR spectroscopy. Using heteronuclear multidimensional techniques, the conformational properties of D1-D4 have been defined at both a global and a local level. Diffusion studies give an average effective radius of 26.2 +/- 0.1 A, approximately 75% larger than that...Expand abstract
- Publication status:
- Publisher copy:
- Copyright date:
Views and Downloads
If you are the owner of this record, you can report an update to it here: Report update to this record