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. 1999 Apr;13(4):381-5.
doi: 10.1023/a:1008393903034.

A novel NMR experiment for the sequential assignment of proline residues and proline stretches in 13C/15N-labeled proteins

M J Bottomley  1 , M J Macias, Z Liu, M Sattler
Affiliations

A novel NMR experiment for the sequential assignment of proline residues and proline stretches in 13C/15N-labeled proteins

M J Bottomley et al. J Biomol NMR. 1999 Apr.

Abstract

A new pulse sequence is described for the sequential assignment of proline residues in 13C/15N-labeled proteins by correlating C delta and C alpha chemical shifts of proline residues with the H alpha chemical shift of the preceding residue. Notably, the experiment can provide the sequential connectivities in poly-proline stretches, which cannot be determined using standard triple resonance experiments. Excellent solvent suppression is achieved by coherence selection via a heteronuclear gradient echo. The new pulse sequence has been successfully applied to the 11 kDa HRDC domain.

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References

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