This title appears in the Scientific Report :
2012
Please use the identifier:
http://dx.doi.org/10.1016/j.jmr.2011.10.019 in citations.
iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein
iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein
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...
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Personal Name(s): | Feuerstein, S. |
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Plevin, M.J. / Willbold, D. / Brutscher, B. | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Journal of magnetic resonance, 214 (2012) S. 329 - 334 |
Imprint: |
Amsterdam [u.a.]
Elsevier
2012
|
Physical Description: |
329 - 334 |
PubMed ID: |
22123230 |
DOI: |
10.1016/j.jmr.2011.10.019 |
Document Type: |
Journal Article |
Research Program: |
Biogenesis of Oncogenic MicroRNAs : from the structure of the microRNA processing complexes to the inhibition of the maturation of human oncogenes High resolution tools to understand the functional role of protein intrinsic disorder BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung Funktion und Dysfunktion des Nervensystems |
Series Title: |
Journal of Magnetic Resonance
214 |
Subject (ZB): | |
Publikationsportal JuSER |
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. |