A New Method to Determine the Transmembrane Conformation of Substrates in Intramembrane Proteolysis by Deep-UV Resonance Raman Spectroscopy.

Autor:	Cooley JW; University of Missouri, Columbia, MO, United States., Abdine A; Icahn School of Medicine at Mount Sinai, New York, NY, United States., Brown M; University of Missouri, Columbia, MO, United States., Chavez J; Icahn School of Medicine at Mount Sinai, New York, NY, United States., Lada B; University of Missouri, Columbia, MO, United States., JiJi RD; University of Missouri, Columbia, MO, United States., Ubarretxena-Belandia I; Icahn School of Medicine at Mount Sinai, New York, NY, United States. Electronic address: iban.ubarretxena@mssm.edu.
Jazyk:	angličtina
Zdroj:	Methods in enzymology [Methods Enzymol] 2017; Vol. 584, pp. 207-228. Date of Electronic Publication: 2016 Dec 09.
DOI:	10.1016/bs.mie.2016.10.030
Abstrakt:	We present a new method based on deep-UV resonance Raman spectroscopy to determine the backbone conformation of intramembrane protease substrates. The classical amide vibrational modes reporting on the conformation of just the transmembrane region of the substrate can be resolved from solvent exchangeable regions outside the detergent micelle by partial deuteration of the solvent. In the presence of isotopically triple-labeled intramembrane protease, these amide modes can be accurately measured to monitor the transmembrane conformation of the substrate during intramembrane proteolysis. (© 2017 Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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