FAST FOLDING OF A PROTOTYPIC POLYPEPTIDE - THE IMMUNOGLOBULIN BINDINGDOMAIN OF STREPTOCOCCAL PROTEIN-G

Citation
J. Kuszewski et al., FAST FOLDING OF A PROTOTYPIC POLYPEPTIDE - THE IMMUNOGLOBULIN BINDINGDOMAIN OF STREPTOCOCCAL PROTEIN-G, Protein science, 3(11), 1994, pp. 1945-1952
Citations number
45
Categorie Soggetti
Biology
Journal title
ISSN journal
09618368
Volume
3
Issue
11
Year of publication
1994
Pages
1945 - 1952
Database
ISI
SICI code
0961-8368(1994)3:11<1945:FFOAPP>2.0.ZU;2-U
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 com plicating features superimposed upon the intrinsic properties of the p olypeptide chain. Collapse to a semicompact state exhibiting partial o rder, reflected in protection factors for ND-NH exchange up to 10-fold higher than that expected for a random coil, occurs within the dead t ime (less than or equal to 1 ms) of the quenched flow apparatus. This is followed by the formation of the fully native state, as monitored b y the fractional proton occupancy of 26 backbone amide groups spread t hroughout the protein, in a single rapid concerted step with a half-li fe of 5.2 ms at 5 degrees C.