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 (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 (< or = 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 degrees C. Study holds ProTherm entries: 12315 Extra Details: folding intermediates; protein folding; quenched-flow deuterium-hydrogen exchange

Submission Details

ID: SdRinVSX4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:43 p.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
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