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1.
Figure 7

Figure 7. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

Crystal structure of the FMO antenna protein complex; the protein is displayed in cartoon mode; BChl a is depicted as a stick mode with gray color.

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

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2.
Figure 3

Figure 3. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

Sequence coverage of ConA by top-down ECD for denatured ConA (24+ charge state, in 50% acetonitrile 50% water 1% formic acid) (top) and for ConA in its near native state (bottom).

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

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3.
Figure 1

Figure 1. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

(a) The layout of Hybrid Qq-FTICR instrument. (b) ECD top-down sequencing by FTICR MS: (1) after selection of one charge state in the quadrupole region and fragmentation in the ICR trap (top); (2) after selection and fragmentation in the FTICR trap (middle); and (3) with no pre-selection by quadrupole or in the ICR trap (bottom).

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

CitationFull text

4.
Figure 2

Figure 2. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

ECD mass spectra of intact protein assemblies: (a) concanavalin A (ConA) from Canavalia ensiformis (Jack bean); (b) FMO antenna protein from green sulfur bacterium Chlorobaculum tepidum; (c) yeast alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae. The insets are native ESI spectra of each protein complex.

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

CitationFull text

5.
Figure 4

Figure 4. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

(a) Normalized abundances of the ECD fragment ions (c ions) from the ADH assembly at different acceleration potentials (ISCID). (b) Atomic displacement parameter (B-factor) plot for the C terminal region of ADH. The B-factor values are from the crystal structure of yeast ADH (PDB id: 2HCY). In the crystal structure, the protein has four different conformations represented by Chain A–D.

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

CitationFull text

6.
Figure 6

Figure 6. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

Native ESI and ECD/CID top-down spectra of the FMO antenna protein complex. (a–c) native ESI spectra of FMO with 0, 10, 20 V ISCID. No fragment ions were observed. (d) ECD spectrum of FMO protein with 15 V ISCID. (e) CID (10 V) spectrum of FMO; no fragment ions were observed. (f) CID (20 V) spectrum of FMO. Multiply charged fragment ions were observed at low m/z.

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

CitationFull text

7.
Figure 5

Figure 5. From: Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-down Studies of Protein Assemblies.

Tetrameric ADH crystal structure color-coded to show the B factor extent. Tetrameric ADH complex was assembled by crystal packing (PDB id: 2HCY). Dimer on the bottom of ADH complex is displayed with the B-factor scheme (the color and width represent the value of B factor) from crystal data (Chain B). In the yeast ADH crystal structure, there are four different conformations for subunit. We compared all B-factor values from different subunit conformations. The best correlation was observed on chain B conformation which was plot in the crystal structure

Hao Zhang, et al. Anal Chem. ;83(14):5598-5606.

CitationFull text

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