Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution
- 12 June 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 366 (2-3), 99-103
- https://doi.org/10.1016/0014-5793(95)00503-2
Abstract
We examined the complementation of various pairs of fragments derived from the streptococcal protein G B1 domain by NMR and CD. Most were not associated; however, one pair of fragments (1–40) and (41–56) interacted sufficiently enoughto regenerate a stable 1:1 complex, K d = 9 × 10−6M. A 2D-NMR analysis showed that the structure of the complex resembled that of native domain. Here we discuss the complementation from the viewpoint of the folding pathway of the protein.Keywords
This publication has 35 references indexed in Scilit:
- Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobinBiochemistry, 1993
- Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein GBiochemistry, 1992
- Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperaturesBiochemistry, 1992
- Dissection of an enzyme by protein engineering: The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activityJournal of Molecular Biology, 1992
- How does protein synthesis give rise to the 3D‐structure?FEBS Letters, 1991
- Iterative schemes for bilinear operators; application to spin decouplingJournal of Magnetic Resonance (1969), 1988
- A New Standard Substance for Calibration of Circular Dichroism: Ammonium d-10-CamphorsulfonateAnalytical Sciences, 1985
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spinsJournal of Magnetic Resonance (1969), 1981
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979