Cooperative folding units of escherichia coli tryptophan repressor.
A previously published computational procedure was used to identify cooperative folding units within tryptophan repressor. The theoretical results predict the existence of distinct stable substructures in the protein chain for the monomer and the dimer. The predictions were compared with experimental data on structure and folding of the repressor and its proteolytic fragments and show excellent agreement for the dimeric form of the protein. The results suggest that the monomer, the structure of which is currently unknown, is likely to have a structure different from the one it has within the context of the highly intertwined dimer. Application of this method to the repressor monomer represents an extension of the computations into the realm of evaluating hypothetical structures such as those produced by threading.
Wallqvist
A
A
Frederick Cancer Research and Development Center, National Cancer Institute, Science Applications International Corporation, Frederick, Maryland 21702 USA.
Lavoie
T A
TA
Chanatry
J A
JA
Covell
D G
DG
Carey
J
J
D001059:Apoproteins / Q000737:chemistry; D001426:Bacterial Proteins; D002942:Circular Dichroism; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism
D001059:Apoproteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D012097:Repressor Proteins; C027190:TRPR protein, E coli