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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
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Globin X: A highly stable intrinsically hexacoordinate globin.
Rifat Farhana1, Ruipeng Lei1, Khoa Pham1
1Department of Chemistry and Biochemistry, Florida International University, Miami, FL, United States of America.
Journal of Inorganic Biochemistry
|September 4, 2022
Summary
Zebrafish hexacoordinate globin X (GbX) exhibits remarkable stability due to its unique structure, including a disulfide bond and heme hexa-coordination. Further determinants contribute to its enhanced thermal and chemical stability.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Novel vertebrate globins possess unique structural features beyond traditional penta-coordinate globins.
- Hexacoordinate globin X (GbX) from Danio rerio (zebrafish) represents a unique class of globins.
Purpose of the Study:
- To elucidate the molecular determinants contributing to the stability of zebrafish hexacoordinate globin X (GbX).
- To characterize the structural stability of GbX using various biophysical techniques.
Main Methods:
- pH-induced and Guanidine Hydrochloride (GuHCl)-induced protein unfolding experiments.
- Differential Scanning Calorimetry (DSC) to determine melting points.
- Native and collision-induced unfolding Ion Mobility-Mass Spectrometry (IM-MS).
Main Results:
- GbX exhibits high stability, with specific mutations (C65A, H90V) affecting unfolding thermodynamics and pH midpoints.
- High melting points (118°C for GbXWT, 107°C for GbXC65A) indicate significant thermal stability.
- IM-MS confirms a native, structured state and two-state unfolding transitions, with GbXWT retaining heme across charge states.
Conclusions:
- Zebrafish GbX possesses inherent stability enhanced by factors beyond disulfide bonds and heme hexa-coordination.
- The protein's structural integrity is robust, as evidenced by thermal, chemical, and mass spectrometry analyses.
- GbX's stability suggests unique functional roles within the vertebrate globin family.
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