The document summarizes a seminar on using magnetic resonance techniques like NMR and EPR spectroscopy to study the structure and dynamics of membrane proteins like Sec14p. The presenter Mary Chely Quiñones discussed using EPR spectroscopy with spin-labeled lipids to study the local environment and dynamics of lipids binding to Sec14p in order to better understand vitamin E disorders.

1. Seminar- Magnetic Resonance as a Tool for Structural Studies of Membrane Proteins
By Ms. Mary Chely Quiñones
First of all, magnetic resonance is the absorption or emission of electromagnetic
radiation by electrons or atomic nuclei in response to the application of certain magnetic
field. This technique can help us understand protein structural and mechanical
information. There are different techniques of magnetic resonance such as: Nuclear
Magnetic Resonance (NMR), Magnetic Resonance Imaging (MRI), Electron
Paramagnetic Resonance (EPR). The NMR exploits the magnetic properties of certain
nuclei. The MRI is used to evaluate the head, the chest, the blood vessels, the
abdomen and pelvis, the bones and joints, and the spine. The EPR is used to study
molecules and ions containing unpaired electrons. In this seminar, I learned that
Sec14p is a phospholipid transfer protein, and that it is useful for vitamin E disorders.
The research of Mary Chely consists of using EPR spectroscopy to study the local
dynamics and the electrostatic microenvironment of a series of spin-labeled lipids
binding to Sec14p. In conclusion, I learned how labels work, and what is needed for the
binding of the label (with the phospholipid) to the Sec14p.
Questions:
1. What does the term “peaks of adsorption” mean?
2. Why is cysteine used for binding?
3. Wouldn’t the homolog protein used in this research give somehow different results from
the expected ones with the original protein?