Work

Binding of Dodecyl Sulfate to Proteins at High Binding Ratios. Possible Implications for the State of Proteins in Biological Membranes

Year: 1970

Type: article

Abstract: A wide variety of proteins have been shown to bind identical amounts of an amphiphile, sodium dodecyl sulfate, on a gram per gram basis at monomer equilibrium concentrations above 0.5 mM. The binding is independent of ionic strength and primarily hydrophobic in nature. Only the monomeric form of the amphiphile binds to proteins, not the micellar form. The application of these results to models for biological membranes and to gel electrophoresis in sodium dodecyl sulfate is discussed.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.66.3.1002

Authors: Jacqueline A. Reynolds, Charles Tanford

Institution: Duke Medical Center

Language: English

Topic: Lipid Membrane Structure and Behavior

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2077085156

FWCI: 10.21

Cites: 14

Cited by: 698

Related to: 10