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1.
Fig. 5

Fig. 5. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Far-UV CD of YshA. The CD of YshAΔ2-20 in either SDS or SDS/DDM was measured at the indicated temperatures (where 95-20° C was heated and then cooled backed down) from 185 to 265 nm. YshAΔ2-20 has a β-sheet-rich secondary structure in SDS/DDM at 20° C.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
2.
Fig. 4

Fig. 4. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Near-UV CD of YshA. The CD of YshAΔ2-20 in either SDS or SDS/DDM was measured at the indicated temperatures (where 95-20° C was heated and then cooled backed down) from 250 to 350 nm. YshAΔ2-20 has a distinct, heat-labile, tertiary order in SDS/DDM at 20° C.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
3.
Fig. 7

Fig. 7. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Structural analysis of lipid-embedded YshAΔ2-20. A) Coomassie-stained gel showing that bilayer-embedded YshAΔ2-20 has a similar migration shift to YshAΔ2-20 folded in SDS/DDM solution. B) The CD was measured for bilayer-embedded YshAΔ2-20 from 190 to 250 nm. The secondary structure of YshAΔ2-20 in a bilayer environment is similar to YshAΔ2-20 in SDS/DDM, but not YshAΔ2-20 in SDS alone.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
4.
Fig. 8

Fig. 8. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Liposome swelling assay. Liposomes (A) or proteoliposomes containing YshAΔ2-20 (B) were treated with isotonic solutions of arabinose (Ara; R(radius) = 0.38 nm), PEG 400 (R = 0.7 nm), or PEG 600 (R = 0.8 nm) while monitoring the OD440 over time.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
5.
Fig. 2

Fig. 2. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Subcellular localization of YshA. Western blots of subcellular fractions from E. coli transformed with either an empty vector (pet24a) or a vector carrying the WT yshA gene. The cytosol (C), the inner membrane (I), and the outer membrane (O). Antibodies specific to YshA showed that YshA localized to the outer membrane. The maltoporin, LamB, was also identified in the outer membrane fraction.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
6.
Fig. 3

Fig. 3. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Electrophoretic mobility shift of folded YshA. A) Outer membrane fraction of E. coli that expressed WT YshA either boiled or not. The Coomassie-stained gel (C) shows total protein and the western blot (W) specifically shows YshA. B) Purified signal peptide deletion mutant YshAΔ2-20 in either SDS or SDS/DDM solution, either boiled or not.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
7.
Fig. 6

Fig. 6. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Liposome flotation assay. Samples of YshAΔ2-20 and/or liposomes were prepared as described in methods and subjected to ultracentrifugation in a sucrose density gradient to determine if YshAΔ2-20 could be inserted into a lipid bilayer. The control samples containing either YshAΔ2-20 in the absence of liposomes or vice-versa were centrifuged under either denaturing conditions (A), or non-denaturing conditions (B). The experimental samples where YshAΔ2-20 and liposomes were prepared together were also centrifuged under denaturing (C) or non-denaturing (D) conditions. YshAΔ2-20 and liposomes are found in the same fractions only under non-denaturing conditions when prepared together.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.
8.
Fig. 1

Fig. 1. From: The prediction and characterization of YshA, an unknown outer membrane protein from Salmonella typhimurium.

Structural prediction of YshA. A) Topology prediction of YshA was performed with the Freeman-Wimley algorithm [7]. The peaks in the β-strand score which indicate the centers of predicted β-strands are circled. B) The sequence of YshA annotated with predicted β-hairpins, predicted N-terminal export signal peptide (predicted by the SignalP server [11]) and signal peptide cleavage site (black triangle). The single underlined residues indicate predicted TM β-strands. The double underlined residues were removed to make the signal peptide deletion mutant, YshAΔ2-20.

Thomas C. Freeman, et al. Biochim Biophys Acta. ;1808(1):287-297.

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