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Results: 3

1.
FIGURE 3

FIGURE 3. From: From the Test Tube to the Cell: Exploring the Folding and Aggregation of a β-Clam Protein.

Urea denaturation curves as a function of incubation time in vitro and in vivo. (A) Urea melt of FlAsH-labeled tetra-Cys CRABP in vitro after sample incubation for the indicated times, monitored by Trp fluorescence; (B) urea melt of FlAsH-labeled P39A tetra-Cys CRABP in vitro after sample incubation for the indicated times, monitored by Trp fluorescence; (C) urea melt of FlAsH-labeled tetra-Cys CRABP in vivo after sample incubation for the indicated times, monitored by FlAsH fluorescence; and (D) urea melt of FlAsH-labeled P39A tetra-Cys CRABP in vivo after sample incubation for the indicated times, monitored by FlAsH fluorescence.

Zoya Ignatova, et al. Biopolymers. ;88(2):157-163.
2.
FIGURE 1

FIGURE 1. From: From the Test Tube to the Cell: Exploring the Folding and Aggregation of a β-Clam Protein.

Design of tetra-Cys CRABP. (A) Backbone structure of CRABP (PDB code 1CBI) showing the position of the tetra-Cys motif in the highly variable Ω-loop. (B) Fluorescence spectra of FlAsH-labeled tetra-Cys CRABP in its native state (folded) and denatured with 8M urea (unfolded). [Figure adapted from Ignatova, Z.; Gierasch, L. M. Proc Natl Acad Sci USA 2004, 101, 523–528.]

Zoya Ignatova, et al. Biopolymers. ;88(2):157-163.
3.
FIGURE 2

FIGURE 2. From: From the Test Tube to the Cell: Exploring the Folding and Aggregation of a β-Clam Protein.

Monitoring aggregation in vivo. (A) Time course of in-cell expression of FlAsH-labeled tetra-Cys CRABP I, P39A tetra-Cys CRABP and chimeras of tetra-Cys CRABP and exon 1 of Huntingtin with 40 and 53 glutamine residues followed at 530 nm.12,14 Cells were pre-loaded with FlAsH before induction of protein expression at time zero. Tetra-Cys CRABP (red) is soluble, P39A tetra-Cys CRABP (purple) partitions 50% into the insoluble fraction, tetra-Cys CRABP HD40 (orange) is 20% in the insoluble fraction, and tetra-Cys CRABP Htt53 (light blue) is isolated only in an insoluble state. For comparison, the fluorescence in all the samples is normalized against the highest fluorescence measured (tetra-Cys CRABP Htt53) and the cell number. (B) Fluorescence microscopy images of E. coli cells expressing P39A tetra-Cys CRABP showing the conversion of the uniformly distributed fluorescence (arising from the soluble state) into hyperfluorescent aggregates localized at the poles of the cells. [Parts of this figure reproduced with permission from Ignatova, Z.; Gierasch, L. M. J Biol Chem 2006, 281, 12959–12967.]

Zoya Ignatova, et al. Biopolymers. ;88(2):157-163.

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