Table 2.

Reduced Dimensionality Experiments without Full Quadrature Detection

Measurement	Sample	Experiment(s)†	Type‡	Ref.
Backbone assignment	mixed disulfide of E. coli glutaredoxin- (C14S) and glutathione	(4,3)-D HACANH	MQ	[47]
Backbone assignment	mixed disulfide of E. coli glutaredoxin- (C14S) and glutathione	(4,3)-D HACANH, (3,2)-D HNCA	IEPs	[48]
Backbone assignment	DnaJ, residues 2-108	(4,3)-D Hα/βCα/β(CO)NH	IEPs	[110]
Backbone assignment	Rhodobacter capsulatus cytochrome c2	(3,2)-D HNCA, HNCO	MQ	[56]
Backbone assignment	Rhodobacter capsulatus ferrocytochrome c2	(3,2)-D HNCO, HN(CO)CA, H(N)COCA, HN(COCA)H, HNCA, HN(CA)CO and HN(CA)H	both	[111]
Backbone assignment	Desulfovibrio vulgaris flavodoxin	(5,3)-{HACA}{CON}H	IEPs	[108]
Backbone assignment	Rhodobacter capsulatus cytochrome c′	(4,3)-D HNCOCA	IEPs	[112]
Backbone assignment	P14A	(4,3)-D HN<CO,CA> with central peaks, originally named COHNNCA	IEPs	[101]
Uridine HN/H6 assignment Cytidine H2N/H6 assignment	leadzyme	(4,3)-D H(NCC)CH	IEPs	[113]
Backbone assignment	N-terminal 63-residue polypeptide fragment of the 434 repressor	(4,3)-D Hα/βCα/β(CO)NH with central peaks	IEPs	[59]
Scalar coupling constants	rhodniin	(3,2)-D DQ/ZQ+SQ-HNCA	both	[104]
Backbone assignment	ubiquitin	(4,3)-D HN(COCA)NH	MQ	[114]
Sidechain carboxylate assignment and titration	N-terminal 63-residue polypeptide fragment of the 434 repressor	(3,2)-D HCCCO2	IEPs	[115]
1H/13C assignments	cyclosporin A	(3,2)-D HC(C)H-COSY with central peaks	IEPs	[116]
Backbone assignment	N-terminal 63-residue polypeptide fragment of the 434 repressor	HNCAHA, plus previously described (4,3)-D HN<CO,CA> and (4,3)-D Hα/βCα/β(CO)NH), with central peaks	IEPs	[102]
Solid state backbone assignments	N-acetyl-Valine-Leucine	(3,2)-D CONCA; (3,2)-D CANCOCA (simultaneous direct acquisition of CO and CA)	IEPs	[117]
Backbone assignments	TM1112	(4,3)-D HNCOCA and HNCACO, as a suite with time-shared 3-D HN[CA/HA] and HN(CO)[CA/HA]	IEPs	[118]
Backbone assignment	GB1	(4,2)-D HN(CO)CAHA, HN(COCA)CAHA; (3,2)-D HN(CO)Cα/β, intra- HN(COCA)Cα/β	both	[57]
Backbone, aliphatic sidechain and aromatic sidechain assignments	Z-domain of Staphylococcal protein A	(4,3)-D HACA(CO)NH and Hα/βCα/βCOHA with central peaks, HCCH-COSY, HCCH-TOCSY; (3,2)-D HBCB(CGCD)HD, TOCSY-relayed-HCH- COSY, plus previously described (4,3)-D Hα/βCα/β(CO)NH, HNCAHA, HN<CO,CA>	IEPs	[103]

^†(n,m)-D indicates that n dimensions of correlations are collected with m independent evolution times. Underlining indicates coevolved nuclei; underlined nuclei grouped in {curly braces} indicate independent sets of coevolved nuclei. (Parentheses) indicate nuclei through which magnetization is passed, without evolving chemical shifts. <Angled brackets> indicate nuclei involved in bifurcated magnetization transfer. C^CO2 represents sidechain carboxylate carbon nuclei. [Square brackets] indicate time-shared evolution of two nuclei, with diagonal slashes separating the nuclei or sets of nuclei that evolve independently. For the meaning of DQ/ZQ+SQ, please see the text. The names for some experiments have been adjusted from the original publications to maintain consistency in nomenclature.

^‡MQ indicates that the coevolution is accomplished by evolving a multiple-quantum coherence; IEPs indicates that the coevolution is accomplished with individual evolution periods.