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Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure

, : Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure. Biochemistry, 262: 333-338

The 1H NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (< 5-.ANG.) connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, C.alpha.H, and C.beta.H protons. It is shown that hirudin has two .beta.-sheets and no .alpha.-helices.


DOI: 10.1021/bi00376a001

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