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Results: 4

1.
Figure 3

Figure 3. From: Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.

Apparent intracellular viscosity as a function of residue number, obtained from 1HN linewidth (red) and TROSY/anti-TROSY (black) analysis on GB1.

Qinghua Wang, et al. Biochemistry. ;50(43):9225-9236.
2.
Figure 1

Figure 1. From: Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.

Effect of protein size on the quality of in-cell NMR spectra. In-cell [1H,15N] HSQC spectra of GB1, NmerA, and GB1-L1-GB1 (dGB1). Spectra were measured with 8, 32, and 16 scans, corresponding to total acquisition times of 10, 40 and 20 minutes for GB1, NmerA, and dGB1, respectively. The boxed regions show sharp peaks arising from flexible NH2 side-chains.

Qinghua Wang, et al. Biochemistry. ;50(43):9225-9236.
3.
Figure 2

Figure 2. From: Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.

Determination of the apparent intracellular viscosity. (A, C) A representative example of a measured (A) 1HN linewidth, Δν, and (C) difference between 15N TROSY and anti-TROSY linewidths, ΔΔνTAT, as a function of the solution viscosity for residue T43 in GB1. Red, blue and green colors correspond to datasets 1, 2 and 3 (Table S1), respectively. Solid lines show the best linear fit obtained using all titration data (A) or only dataset 1 (C). (B, D) Histograms showing Δν (B) and ΔΔνTAT (D) as a function of GB1 residue number. Colors indicate the bulk viscosity in solution from lowest (red) to highest (yellow). In-cell data are shown by black and labeled.

Qinghua Wang, et al. Biochemistry. ;50(43):9225-9236.
4.
Figure 4

Figure 4. From: Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.

Effect of intracellular environments and molecular crowding on protein mobility. (A) Average 1HN linewidths in lysate samples of GB1, NmerA, Ubi3A (U3A in the figure), and dGB1 (red), ubiquitin (green), and average 1HN linewidths (black) obtained from glycerol titrations of GB1 and dGB1 lysates from datasets 2 and 3 (Table S1) as a function of an apparent molecular weight, MW app = MWη/η0, where MW, η, and η0 are the protein molecular weight, the apparent sample viscosity, and the viscosity of water, respectively. A solid black line is the best linear fit of GB1/dGB1 glycerol titrations. (B) Average 1HN linewidths for GB1 and dGB1 (blue), and NmerA (red) lysate samples in the presence of 100 and 200 g/L BSA as a function of an apparent molecular weight, MW app = MWη/η0, where MW, η, and η0 are a protein molecular weight, the bulk viscosity and the viscosity of water, respectively. A solid black line is the best linear fit of GB1/dGB1 glycerol titrations (same as in Fig. 4A). (C) Histograms showing experimental 1HN linewidths, Δν, as a function of NmerA residue number. Colors indicate viscosity in solution from lowest (red) to highest (yellow). Horizontal lines show the average 1HN linewidths for in-cell GB1 and dGB1 samples. A black solid line shows theoretically predicted NmerA linewidths expected for intracellular environment 11 times as viscous as water.

Qinghua Wang, et al. Biochemistry. ;50(43):9225-9236.

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