Nmr
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Transcript of Nmr
Francisco J Fuster
RISE Program
Seminar Summary
Magnetic resonance as a tool for structural studies of membrane proteins:
In this investigation, EPR (electron paramagnetic resonance) was used for the spin
labeling of membrane proteins in order to get a reading in terms of mobility of that
protein. NO (nitric oxide) was used to remove the free electron in order to use it for
labeling. When exposed to a magnetic field the electron was removed and added to
sulfur in the protein sfh1p. This protein was used because the natural sec14p protein
was too unstable at high concentrations. The sfh1p supposedly has similar
characteristics and functions as the sec14p. The main function of the sec14p is for
signal transduction, transport and organelle biological activity regulation. However, the
sfh1p cycles the lipids of the membrane. After the EPR was done, then the NMR
(nuclear magnetic resonance) was used to locate the spin labeled sulfur in the protein.
The readings were determines by the position of the label on the protein that
determined the mobility of the protein. The faster the mobility, then the more possible
biological activities took place. This is a type of signal transduction. The experimentation
was executed “In vitro” maintaining constant pH and temperature because these
proteins may be easily denaturalized by any slight change in any of these factors.