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Details

Protein Quality Control in Bacterial Cells: Integrated Networks of Chaperones and ATP-Dependent Proteases.

DE200415006567

Publication Date	2003
Personal Author	Flanagan, J. M.; Bewley, M. C.
Page Count	60
Abstract	It is generally accepted that the information necessary to specify the native, functional, three-dimensional structure of a protein is encoded entirely within its amino acid sequence; however, efficient reversible folding and unfolding is observed only with a subset of small single-domain proteins. Refolding experiments often lead to the formation of kinetically-trapped, misfolded species that aggregate, even in dilute solution. In the cellular environment, the barriers to efficient protein folding and maintenance of native structure are even larger due to the nature of this process.
Keywords	Proteins Cells(Biology) Bacteria Amino acids Genetic engineering Diseases Mitochondria Polypeptides Quality control Removal Residues Ribosomes Synthesis
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Brookhaven National Lab., Upton, NY. Biology Dept.; Department of Energy, Washington, DC.
Supplemental Notes	Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200418

Protein Quality Control in Bacterial Cells: Integrated Networks of Chaperones and ATP-Dependent Proteases.

Protein Quality Control in Bacterial Cells: Integrated Networks of Chaperones and ATP-Dependent Proteases.
DE200415006567

Publication Date	2003
Personal Author	Flanagan, J. M.; Bewley, M. C.
Page Count	60
Abstract	It is generally accepted that the information necessary to specify the native, functional, three-dimensional structure of a protein is encoded entirely within its amino acid sequence; however, efficient reversible folding and unfolding is observed only with a subset of small single-domain proteins. Refolding experiments often lead to the formation of kinetically-trapped, misfolded species that aggregate, even in dilute solution. In the cellular environment, the barriers to efficient protein folding and maintenance of native structure are even larger due to the nature of this process.
Keywords	Proteins Cells(Biology) Bacteria Amino acids Genetic engineering Diseases Mitochondria Polypeptides Quality control Removal Residues Ribosomes Synthesis
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Brookhaven National Lab., Upton, NY. Biology Dept.; Department of Energy, Washington, DC.
Supplemental Notes	Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200418