NMR
Please explain in a few sentences how the experimental structure of a protein can be derived by NMR.
Why does protein NMR always try to use the most powerful (high magnet field) NMR spectrometer available?
Why do people label their proteins with 13C or 15N when solving the structure by NMR.
When you retrieve an NMR structure of a protein from the protein databank then you often receive an ensemble of structures and not a single structure. Why is this the case?
What happens to an NMR spectrum if you exchange hydrogen atoms against deuterium atom? What can you learn from this, when you do this with a folded protein (hydrogen-deuterium exchange experiment)?
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