Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G


Abstract

The folding of the small (56 residues) highly stable B1 immunoglobulin binding domain (GBl) of streptococcal protein G has been investigated by quenched-flow deuterium-hydrogen exchange. This system represents a para- digm for thestudy 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 to10-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.

Submission Details

ID: 9MX7HECt3

Submitter: Marie Ary

Submission Date: March 8, 2017, 10:59 a.m.

Version: 1

Publication Details
Kuszewski J;Clore GM;Gronenborn AM,Protein Sci (1994) Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G. PMID:7703841
Additional Information

Number of data points 2
Proteins Protein Gβ1
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: [GdmCl]m ; Experimental Assay: ΔG(H2O)
Libraries [GdmCl]m and ΔG(H2O) for WT GB1
Sequence Assay Result Units