Amino acid type-selective backbone 1H-15N-correlations for Arg and Lys.
Four novel amino acid type-selective triple resonance experiments to identify the backbone amino proton and nitrogen resonances of Arg and Lys and of their sequential neighbors in (13C,15N)-labeled proteins are presented: the R(i+1)-HSQC and R(i,i+1)-HSQC select signals originating from Arg side chains, the K(i+1)-HSQC and K(i,i+1)-HSQC select signals originating from Lys side chains. The selection is based on exploiting the characteristic chemical shifts of a pair of carbon atoms in Arg and Lys side chains using selective 90 degree pulses. The new experiments are recorded as two-dimensional 1H-15N-correlations and their performance is demonstrated with the application to a protein domain of 83 amino acids.
Schubert
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M
Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
Oschkinat
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Schmieder
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D000818:Animals; D001120:Arginine / Q000737:chemistry*; D002250:Carbon Radioisotopes / Q000737:chemistry; D002645:Chickens; D008239:Lysine / Q000737:chemistry*; D008433:Mathematics; D015394:Molecular Structure; D009590:Nitrogen Radioisotopes / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry; D036224:Receptor, EphB4; D036081:Receptors, Eph Family
D002250:Carbon Radioisotopes; D009590:Nitrogen Radioisotopes; D011506:Proteins; D011522:Protons; D001120:Arginine; D020794:Receptor Protein-Tyrosine Kinases; D036224:Receptor, EphB4; D036081:Receptors, Eph Family; D008239:Lysine