TY  - JOUR
AU  - Feuerstein, S.
AU  - Plevin, M.J.
AU  - Willbold, D.
AU  - Brutscher, B.
TI  - iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein
JO  - Journal of magnetic resonance
VL  - 214
SN  - 1090-7807
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-19969
SP  - 329 - 334
PY  - 2012
N1  - 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.
AB  - 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.
KW  - Algorithms
KW  - Magnetic Resonance Spectroscopy: methods
KW  - Proteins: chemistry
KW  - Proteins: ultrastructure
KW  - Software
KW  - Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:22123230
UR  - <Go to ISI:>//WOS:000299656400043
DO  - DOI:10.1016/j.jmr.2011.10.019
UR  - https://juser.fz-juelich.de/record/19969
ER  -