Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G
Open Access
- 1 November 1994
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 3 (11), 1945-1952
- https://doi.org/10.1002/pro.5560031106
Abstract
The folding of the small (56 residues) highly stable B1 immunoglobulin binding domain (GB1) of streptococcal protein G has been investigated by quenched‐flow deuterium‐hydrogen exchange. This system represents a paradigm for the study of protein folding because it exhibits no complicating features superimposed upon the intrinsic properties of the polypeptide chain. Collapse to a semicompact state exhibiting partial order, reflected in protection factors for ND‐NH exchange up to 10‐fold higher than that expected for a random coil, occurs within the dead time (≤1 ms) of the quenched flow apparatus. This is followed by the formation of the fully native state, as monitored by the fractional proton occupancy of 26 backbone amide groups spread throughout the protein, in a single rapid concerted step with a half‐life of 5.2 ms at 5 °C.Keywords
This publication has 41 references indexed in Scilit:
- How does a protein fold?Nature, 1994
- Amide Hydrogen Exchange in a Highly Denatured State: Hen Egg-white Lysozyme in UreaJournal of Molecular Biology, 1994
- Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine HydrochlorideJournal of Molecular Biology, 1994
- Formation of a Hydrophobic Cluster in Denatured Bovine Pancreatic Trypsin InhibitorJournal of Molecular Biology, 1994
- Detection of Transient Protein Folding Populations by Mass SpectrometryScience, 1993
- Identification of the Contact Surface of a Streptococcal Protein G Domain Complexed with a Human Fc FragmentJournal of Molecular Biology, 1993
- Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopyBiochemistry, 1993
- A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagramsJournal of Magnetic Resonance (1969), 1991
- Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteinsJournal of Magnetic Resonance (1969), 1990
- Effects of denaturants on amide proton exchange rates: a test for structure in protein fragments and folding intermediatesBiochemistry, 1986