Citation: ZHANG Li-Yu, TANG Ke-Qi, HU Jun. Investigation of Conformational Changes of Hemoglobin at Different pH Values and in Different Alcohol Solutions by Electrospray Ionization-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry[J]. Chinese Journal of Analytical Chemistry, ;2021, 49(8): 1335-1341. doi: 10.19756/j.issn.0253-3820.211021 shu

Investigation of Conformational Changes of Hemoglobin at Different pH Values and in Different Alcohol Solutions by Electrospray Ionization-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry

School of Materials Science and Chemical Engineering, Institute of Mass Spectrometry, Ningbo University, Ningbo 315211, China

Corresponding author: TANG Ke-Qi, HU Jun,
Received Date: 11 January 2021
Revised Date: 5 May 2021

Protein, as one of the important biomolecules, plays important roles in many biological processes. Studies have shown that the function of the protein is closely related to its structure. Therefore, elucidating the structure changes of the protein in a given biological environment is one of the main ways to understand its biological function in a specific process. In this work, a high resolution mass spectrometry (MS) combined with ion mobility spectrometry (IMS) was used to study the conformation changes of hemoglobin under different conditions, such as different pH values and different solvents. The result showed that the structure of hemoglobin changed significantly at pH=4 with observed heme drop. Moreover, the ion mobility of the hemoglobin ions increased as the decrease of pH values, indicating the unfolding of the protein under the acidic solution conditions. By measuring the change of ion mobility, the unfolding of hemoglobin at different pH values was determined. Also the structural changes of hemoglobin ions as the change of the charge states at the same pH values were investigated and it was found that the structure of the hemoglobin became more extended as the increase of the protein charge state. In addition, it was found that the structure of the hemoglobin was also significantly affected by the type and the concentration of alcohol in the solvent. Specifically, the structure of hemoglobin in 50% methanol in water was about the same as the structure in 40% of ethanol aqueous solution. It was also found that the structure of hemoglobin collapsed in high concentration of alcohol solution, which made the structure of hemoglobin in high concentration of alcohol solution more compact.
- Hemoglobin,
- Electrospray ionization-trapped ion mobility spectrometry-time-of-flight mass spectrometry,
- Folding state,
- Conformation
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