Results: 5

1.
Figure 1

Figure 1. From: Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability using Mass Spectrometry.

Schematic representation of the slow histidine H/D exchange protocol developed here.

Duc T. Tran, et al. Anal Chem. ;84(3):1653-1660.
2.
Figure 5

Figure 5. From: Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability using Mass Spectrometry.

Representative Histidine H/D exchange data obtained from a His-120 containing peptide of superoxide dismutase 1 (SOD-1) in the presence (● and solid line) and absence (○ and dotted line) of added Zn2+.

Duc T. Tran, et al. Anal Chem. ;84(3):1653-1660.
3.
Figure 3

Figure 3. From: Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability using Mass Spectrometry.

Slow histidine H/D exchange data for BCA II. Data obtained on a peptide containing histidine residues, His-118 and His-121, is shown in (A) and data obtained for a peptide containing histidine residues, His-93, His-95 and His-96 is shown in (B). The dotted arrows indicate C1/2 values. The solid lines represent the best fit of the data to equation (1), with the data in each transition being fit separately.

Duc T. Tran, et al. Anal Chem. ;84(3):1653-1660.
4.
Figure 2

Figure 2. From: Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability using Mass Spectrometry.

Slow histidine H/D exchange data for Rnase A. Data obtained for a His-48-containing peptide of sequence, VHESLADVQAVCSQK, is shown in (A). The solid line represents the best fit of the data to equation (1), the dotted arrow indicates C1/2 value, the arrows labeled “1” and “2” indicate the data points for which the raw mass spectral data is shown in (B) and (C), respectively.

Duc T. Tran, et al. Anal Chem. ;84(3):1653-1660.
5.
Figure 4

Figure 4. From: Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability using Mass Spectrometry.

Slow histidine H/D exchange data for Hb and the Hb-Hp complex. Data obtained on His-120 containing peptide from the α chain of Hb after 5 days (○ and ●) and 11 days (▽ and ▼) in the presence (○ and ▽) and absence (● and ▼) of Hp is shown in (A). Similar data obtained on a His-92 containing peptide from the β chain of Hb in the presence and absence of Hp is shown in (B). The lines represent best fit of each data set to equation (1).

Duc T. Tran, et al. Anal Chem. ;84(3):1653-1660.

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