title: iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered proteins.
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.
authors: Institut de Biologie Structurale, Université Grenoble 1, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
authors: Sophie
authors: S
authors: Feuerstein
authors: Michael J
authors: MJ
authors: Plevin
authors: Dieter
authors: D
authors: Willbold
authors: Bernhard
authors: B
authors: Brutscher
mesh_terms: D000465:Algorithms; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D012984:Software
chemical_list: D011506:Proteins