Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution.
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 enough to regenerated a stable 1:1 complex, Kd = 9 x 10(-6) M. 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.
Kobayashi
N
N
Institute of Applied Biochemistry, University of Tsukuba, Japan.
Honda
S
S
Yoshii
H
H
Uedaira
H
H
Munekata
E
E
D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions; D014867:Water
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D010446:Peptide Fragments; D012996:Solutions; D014867:Water