Linda Randall

University of Missouri - Columbia

Projects

Identification of covalent modification of SecA

Lead Institution

University of Missouri - Columbia

Principal Investigator

Linda Randall

Project type

Exploratory Research

SecA is the peripherally membrane-bound ATPase that is part of the translocon that mediates the export of proteins from the bacterial cytoplasm and outer membrane. In vivo 50% of the SecA is found…

Determination of the peptide-binding sites on the bacterial chaperone protein SecB

Lead Institution

University of Missouri - Columbia

Principal Investigator

Linda Randall

Project type

Exploratory Research

The chaperone protein SecB is required for the efficient export of certain proteins across the periplasmic membrane of E.coli. SecB promotes export by binding to the proteins and delivering them to…

Identification of the SecB residue that is labeled by methanethiosulfonate

Lead Institution

University of Missouri - Columbia

Principal Investigator

Linda Randall

Project type

Exploratory Research

Aim: To identify the residue of SecB that is labeled by methanethiosulfonate (MTSL), a stable nitroxide spin label. SecB, a small tetrameric cytosolic chaperone in E.coli, facilitates the export…