%0 Journal Article
%A Feuerstein, S.
%A Plevin, M.J.
%A Willbold, D.
%A Brutscher, B.
%T iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein
%J Journal of magnetic resonance
%V 214
%@ 1090-7807
%C Amsterdam [u.a.]
%I Elsevier
%M PreJuSER-19969
%P 329 - 334
%D 2012
%Z We thank I. Ayala (IBS Grenoble) for help with the production of the protein samples used for this study, and S. Hoffmann (FZ Julich) for stimulating discussion on the NS5A project. This work has been supported in part by grants from the European Commission (FP7-I3-BIO-NMR contract No. 261862, FP7-ITN-IDPbyNMR contract No. 264257, and FPR-IRG-2008 contract No. 231082), and financial support from ARC to M.J.P. and from CEA to S.F.
%X 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.
%K Algorithms
%K Magnetic Resonance Spectroscopy: methods
%K Proteins: chemistry
%K Proteins: ultrastructure
%K Software
%K Proteins (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:22123230
%U <Go to ISI:>//WOS:000299656400043
%R 10.1016/j.jmr.2011.10.019
%U https://juser.fz-juelich.de/record/19969