Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor.
Subdomain-size proteolytic fragments of Escherichia coli trp repressor have been produced that assemble in defined order to regenerate fully native dimers. By characterization of the secondary and tertiary structures of isolated and recombined fragments, the structure of assembly intermediates can be correlated with the kinetic folding pathway of the intact repressor deduced from spectroscopic measurement of folding rates. The nativelike structure of these intermediates provides further evidence that protein folding pathways reflect the stabilities of secondary structural units and assemblies found in the native state. The proteolytic method should be generally useful in adding structural detail to spectroscopically determined folding mechanisms.
Tasayco
M L
ML
Chemistry Department, Princeton University, NJ 08544.
Carey
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008961:Models, Structural; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D012097:Repressor Proteins; C027190:TRPR protein, E coli; D029968:Escherichia coli Proteins