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Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments
Author(s) -
Logan Timothy M.,
Olejniczak Edward T.,
Xu Robert X.,
Fesik Stephen W.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81517-p
Subject(s) - heteronuclear molecule , side chain , chemistry , chain (unit) , stereochemistry , nuclear magnetic resonance spectroscopy , organic chemistry , physics , polymer , astronomy
Two multidimensional heteronuclear NMR experiments are described for assigning the resonances in uniformly 15 N‐ and 13 C‐labeled proteins. In one experiment (HCNH‐TOCSY), the amide nitrogen and proton are correlated to the side‐chain protons and carbons of the same and preceding residue. In a second triple resonance experiment (HC(CO)NH‐TOCSY), the amide nitrogen and proton of one residue is correlated exclusively with the side‐chain proton and carbon resonances of the preceding residue by transferring magnetization through the intervening carbonyl. The utility of these two experiments for making sequential resonance assignments in proteins is illustrated for [U‐ 15 N, 13 C]FKBP (107 residues) complexed to the immunosuppressant, ascomycin.