Protein Structure



What can we learn about a protein from NMR?

1) Solve a structure

The standard approach to NMR protein structure.


2) Details about protein motion, interactions, etc.

Mapping interactions by chemical shift changes. Mapping interactions by NOE (relaxation and dipolar coupling).
Residual dipolar coupling (RDC) for relative bond orientation. Great potential for structure work. pH titrations (chemical shift).

Rotational motion of side chains.

Mobility of protein domains by relaxation. Difficult to interpret physically because of complexity of relaxation mechanisms.


Let's say you have 3 mg of a 100-residue protein, in 0.3 ml of buffer...

1D spectrum of a small protein


2D NOESY spectrum of a protein


Works well for ~ 100 amino acids, but starts to look hairy for larger proteins...


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