Charge Isomers of Myelin Basic Protein: Structure and Interactions with Membranes, Nucleotide Analogues, and Calmodulin
Author Information
Author(s): Wang Chaozhan, Neugebauer Ute, Bürck Jochen, Myllykoski Matti, Baumgärtel Peter, Popp Jürgen, Kursula Petri
Primary Institution: Department of Biochemistry, University of Oulu, Oulu, Finland
Hypothesis
The study investigates the structural and functional differences between two charge isomers of myelin basic protein (MBP), rmC1 and rmC8, and their interactions with ligands.
Conclusion
The results indicate that while both isoforms have similar properties, rmC8 is impaired in both ligand binding and structure compared to rmC1.
Supporting Evidence
- The study provides further proof that rmC8 is deficient both in structure and function compared to rmC1.
- Both isoforms present X-ray scattering compatible with an intrinsically disordered molecule.
- Raman spectroscopy indicates that the structures of rmC1 and rmC8 are essentially identical in lyophilized samples.
- The binding of nucleoside triphosphates was inhibited by the presence of calmodulin.
Takeaway
This study looks at two forms of a protein important for the nervous system and finds that one form doesn't work as well as the other when interacting with other molecules.
Methodology
The study used various biochemical and biophysical methods including size exclusion chromatography, calorimetry, surface plasmon resonance, small angle X-ray and neutron scattering, and circular dichroism spectroscopy.
Digital Object Identifier (DOI)
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