Hauptseite > Publikationsdatenbank > iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein |
Journal Article | PreJuSER-19969 |
; ; ;
2012
Elsevier
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.jmr.2011.10.019
Abstract: An experiment, iHADAMAC, is presented that yields information on the amino-acid type of individual residues in a protein by editing the (1)H-(15)N correlations into seven different 2D spectra, each corresponding to a different class of amino-acid types. Amino-acid type discrimination is realized via a Hadamard encoding scheme based on four different spin manipulations as recently introduced in the context of the sequential HADAMAC experiment. Both sequential and intra-residue HADAMAC experiments yield highly complementary information that greatly facilitate resonance assignment of proteins with high frequency degeneracy, as demonstrated here for a 188-residue intrinsically disordered protein fragment of the hepatitis C virus protein NS5A.
Keyword(s): Algorithms (MeSH) ; Magnetic Resonance Spectroscopy: methods (MeSH) ; Proteins: chemistry (MeSH) ; Proteins: ultrastructure (MeSH) ; Software (MeSH) ; Proteins ; J ; NMR (auto) ; Protein (auto) ; IDP (auto) ; Sequential resonance assignment (auto) ; HADAMAC (auto)
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