Work

FlgM gains structure in living cells

Year: 2002

Type: article

Abstract: Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that FlgM gains structure inside living Escherichia coli cells and under physiologically relevant conditions in vitro, i.e., in solutions containing high concentrations (>/=400 g/liter) of glucose, BSA, or ovalbumin. Structure formation represents solute-induced changes in the equilibrium between the structured and disordered forms of FlgM. The results provide insight into how the environment of intrinsically disordered proteins could dictate their structure and, in turn, emphasize the relevance of studying proteins in living cells and in vitro under physiologically realistic conditions.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.202331299

Authors: Matthew M. Dedmon, Chetan N. Patel, Gregory B. Young, Gary J. Pielak

Institutions: University of North Carolina at Chapel Hill, UNC Lineberger Comprehensive Cancer Center

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, American Chemical Society Petroleum Research Fund

OpenAlex ID: W1995838356

FWCI: 3.88

Cites: 27

Cited by: 320

Related to: 10