A novel NMR experiment for the sequential assignment of proline residues and proline stretches in 13C/15N-labeled proteins.
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.
Bottomley
M J
MJ
European Molecular Biology Laboratory, Heidelberg, Germany.
Macias
M J
MJ
Liu
Z
Z
Sattler
M
M
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D004265:DNA Helicases / Q000737:chemistry*; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry; D011392:Proline; D017433:Protein Structure, Secondary; D053484:RecQ Helicases; D029701:Saccharomyces cerevisiae Proteins
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; C011083:polyproline; D011392:Proline; C090472:SGS1 protein, S cerevisiae; D004265:DNA Helicases; D053484:RecQ Helicases