- Sprache
-
Englisch
- Identifier
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1107018013
Beteiligte Personen und Organisationen
- URN
- Rechteinformation
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
26.01.2023, 13:57 MEZ
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Chaperone-assisted folding of newly synthesized proteins in the cytosol
Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
Functional dissection of trigger factor and DnaK : interactions with nascent polypeptides and thermally denatured proteins
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Three-state equilibrium of Escherichia coli trigger factor
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
L23 protein functions as a chaperone docking site on the ribosome
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
Functional dissection of trigger factor and DnaK : interactions with nascent polypeptides and thermally denatured proteins
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Three-state equilibrium of Escherichia coli trigger factor
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
L23 protein functions as a chaperone docking site on the ribosome
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
Functional dissection of trigger factor and DnaK : interactions with nascent polypeptides and thermally denatured proteins
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Three-state equilibrium of Escherichia coli trigger factor
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes