Figure 1. Fluorescence-based assay for measuring TMD embedding. (A) The amino acid sequence of β3 TMD tail peptide. The red arrow indicates the site of acid cleavage, and black arrows indicate bimane labeling sites. (B) Embedding changes of TMD. Yellow pentagons represent bimanes, and the structure of monobromobimane and TMD tilt angle are also shown. (C) Structure of β3 TMD, with side chains of Leu694 and Ile721 indicated. (D) Negative-stain electron microscopic image of nanodiscs containing β3 TMD tail peptide. Arrows indicate nanodiscs. Bar, 50 nm. (E) Emission spectra of nanodiscs containing β3 TMD tail bimane labeled at L694C (L694C-bimane nanodisc) in the presence or absence of K716E mutation (left). The same peptides in the presence of 2% SDS are shown on the right. Data are representative of three independent experiments.
Figure 1.

Fluorescence-based assay for measuring TMD embedding. (A) The amino acid sequence of β3 TMD tail peptide. The red arrow indicates the site of acid cleavage, and black arrows indicate bimane labeling sites. (B) Embedding changes of TMD. Yellow pentagons represent bimanes, and the structure of monobromobimane and TMD tilt angle are also shown. (C) Structure of β3 TMD, with side chains of Leu694 and Ile721 indicated. (D) Negative-stain electron microscopic image of nanodiscs containing β3 TMD tail peptide. Arrows indicate nanodiscs. Bar, 50 nm. (E) Emission spectra of nanodiscs containing β3 TMD tail bimane labeled at L694C (L694C-bimane nanodisc) in the presence or absence of K716E mutation (left). The same peptides in the presence of 2% SDS are shown on the right. Data are representative of three independent experiments.

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