HACACO revisited: residual dipolar coupling measurements and resonance assignments in proteins.
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 tool 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.
Cicero
Daniel O
DO
Department of Chemical Science and Technology, University of Rome "Tor Vergata," Italy.
Contessa
Gian Marco
GM
Paci
Maurizio
M
Bazzo
Renzo
R
D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
D001426:Bacterial Proteins; D002247:Carbon Isotopes