Seminar  mary chely 2010
Upcoming SlideShare
Loading in...5
×

Like this? Share it with your network

Share
  • Full Name Full Name Comment goes here.
    Are you sure you want to
    Your message goes here
    Be the first to comment
    Be the first to like this
No Downloads

Views

Total Views
229
On Slideshare
229
From Embeds
0
Number of Embeds
0

Actions

Shares
Downloads
0
Comments
0
Likes
0

Embeds 0

No embeds

Report content

Flagged as inappropriate Flag as inappropriate
Flag as inappropriate

Select your reason for flagging this presentation as inappropriate.

Cancel
    No notes for slide

Transcript

  • 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?