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AbstractAbstract
[en] 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 deg. 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
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Copyright (c) 2001 Kluwer Academic Publishers; Country of input: International Atomic Energy Agency (IAEA)
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Journal Article
Journal
Journal of Biomolecular NMR; ISSN 0925-2738;
; v. 20(4); p. 379-384

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