The revisited version of the HACACO experiment here presented, is more robust and straightforward to implement and continues to be, to a greater extent, a convenient too] for protein backbone resonance assignment. Additionally, it turns out to be a sensitive and accurate method to measure C-alpha-H-alpha residual dipolar couplings (RDCs). The performance of our new pulse scheme for measurement of RDCs was tested on two proteins with different secondary structures: one characterized by a high beta-sheet content, the second dominated by the presence of alpha-helices. In both examples the new method provided significantly more accurate data, compared to all previously published 3D techniques. (c) 2006 Elsevier Inc. All rights reserved.
Cicero, D.o., Contessa, G., Paci, M., Bazzo, R. (2006). HACACO revisited: Residual dipolar coupling measurements and resonance assignments in proteins. JOURNAL OF MAGNETIC RESONANCE, 180(2), 222-228 [10.1016/j.jmr.2006.02.016].
HACACO revisited: Residual dipolar coupling measurements and resonance assignments in proteins
CICERO, DANIEL OSCAR;PACI, MAURIZIO;
2006-01-01
Abstract
The revisited version of the HACACO experiment here presented, is more robust and straightforward to implement and continues to be, to a greater extent, a convenient too] for protein backbone resonance assignment. Additionally, it turns out to be a sensitive and accurate method to measure C-alpha-H-alpha residual dipolar couplings (RDCs). The performance of our new pulse scheme for measurement of RDCs was tested on two proteins with different secondary structures: one characterized by a high beta-sheet content, the second dominated by the presence of alpha-helices. In both examples the new method provided significantly more accurate data, compared to all previously published 3D techniques. (c) 2006 Elsevier Inc. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
