Exclusively heteronuclear (13) C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDPs).
Carbon-13 direct-detection NMR methods have proved to be very useful for the characterization of intrinsically disordered proteins (IDPs). Here we present a suite of experiments in which amino-acid-selective editing blocks are encoded in CACON- and CANCO-type sequences to give (13) C-detected spectra containing correlations arising from a particular type or group of amino acid(s). These two general types of experiments provide the complementary intra- and inter-residue correlations necessary for sequence-specific assignment of backbone resonance frequencies. We demonstrate the capabilities of these experiments on two IDPs: fully reduced Cox17 and WIP(C) . The proposed approach constitutes an independent strategy to simplify crowded spectra as well as to perform sequence-specific assignment, thereby demonstrating its potential to study IDPs.
Bruker BioSpin GmbH, 76287 Rheinstetten, Germany.
Wolfgang
W
Bermel
Ivano
I
Bertini
Jordan
J
Chill
Isabella C
IC
Felli
Noam
N
Haba
Vasantha
V
Kumar M V
Roberta
R
Pierattelli
D000596:Amino Acids / Q000032:analysis*; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy; D011506:Proteins / Q000737:chemistry*
D000596:Amino Acids; D002247:Carbon Isotopes; D011506:Proteins