. Author manuscript; available in PMC: 2011 Nov 1.

Published in final edited form as: Prog Nucl Magn Reson Spectrosc. 2010 Jul 30;57(4):381–419. doi: 10.1016/j.pnmrs.2010.07.001

Table 3.

Full Quadrature Reduced Dimensionality Experiments

Measurement	Sample	Experiment(s)^†	Time^‡ (hrs.)	Ref.
NOE-derived distance restraints	Rhodobacter capsulatus ferrocytochrome c₂	(4,3)-D ¹³C/¹⁵N-NOESY (4,3)-D ¹⁵N/¹⁵N-NOESY	not given	[119]
Backbone assignment	residues 1-68 of merA from Ralstonia metallidurans CH34	(3,2)-D HNCA, HN(CO)CA, HN(CA)CB, HN(COCA)CB, HN(CA)HA, HN(COCA)HA	14	[50]
Backbone assignment	1.5 mM ubiquitin	(3,2)-D HNCA, HN(CO)CA (4,2)-D HACANH	not given	[55]
Solid-state backbone assignment	histidine	(3,2)-D MAS NCC	not given	[128]
Backbone assignment	2 mM ubiquitin	(5,2)-D HACACONH	2.3	[52]
Backbone assignments	1.5 mM ubiquitin 1.1 mM 21 kDa bovine S100A1	(4,2)-D HNCACB and HN(CO)CACB, with C^α and C^βcoevolved as an MQ coherence producing only the DQ (C^α+C^β) peak	Not given	[120]
Backbone assignments	1.5 mM ubiquitin	(3,2)-D HNCO, HNCA, HN(CO)CA, H(N)COCA; (4,2)-D HNCOCA (all MQ)	not given	[121]
Backbone and sidechain assignments	1.4 mM ubiquitin	(3,2)-D HNCO, HNCACB, HN(CO)CACB, HN(CA)CO, HNCA, HN(CO)CA, CBCANH, CBCA(CO)NH, C(CCO)NH, H(CCCO)NH	18	[129]
Backbone and C^β assignment	2 mM ubiquitin, 1 mM TT212	(5,2)-D intra-HACACONN and HACACONH; (5,3)-D intra-<HACA,CO>NH and HACACONH; (4,3)-D intra-<CBCA,CO>NH and CBCACONH	42.6, 62.6	[122]
Backbone and sidechain assignments	1 mM 17 kDa ER75, 1 mM 13 kDa PfR13, 2 mM ubiquitin	(4,2)-D HCCH; (4,3)-D C^α/^βC^α(CO)NH, L- HN(CO)C^α/βC^α, HNC^α/βC^α and L-HNC^α/βC^α; (5,3)-D H^α/^βC^α/^βC^α(CO)NH and HCCCH; (6,3)-D H^α/βC^α/βC^αCONH	224, 32, 68.8	[124]
Backbone and sidechain assignments [also reported structures using non-GFT time-shared NOESY]	8 targets from the NESH consortium, at ~1 mM each	(4,3)-D H^α/βC^α/β(CO)NH and HCCH [plus previously published (4,3)-D C^α/βC^α(CO)NH, L- HN(CO)C^α/βC^α; and (5,2)-D HACACONH]	26 to 214	[130]
Structure determination: backbone assignments by previously published protocols; distance constraints from GFT NOESY	1 mM 14 kDa YqfB	(4,3)-D [HC^ali/HN]- NOESY-[CH^ali/NH], which is a time-shared NOESY experiment detecting HC^ali HC^ali, HN HC^ali HC^ali HN and HN HN [assignment by previously published experiments]	16.9+, 39	[125]
Dynamics of aromatic rings	21 kDa HR41, 13 kDa MAR11	(4,3)-D L-HCCH and L- TROSY-HCCH	24, 0.42	[131]
Backbone assignments	0.8 mM 17 kDa yqbG, 13.5 kDa rps24e, 8 kDa protein Z-domain, ubiquitin, 13.5 kDa rps24e	various combinations of (5,3)-D HN{NCO} {C^α/βC^α}, intra-HN{<N,CO>} {C^α/βC^α}, intra-HN{<N,CO>} {C^α/βH^α}, {H^αC^α}{CON}NH HN{NC^α}{C^α/βC^α}, HN{N(CO)C^α}{C^α/βC^α} and (6,3)-D {H^α/βC^α/βCα}{CON}NH, with and without L-optimization and/or TROSY	7 to 44	[109]
Residual dipolar couplings	8 kDa protein Z- domain	(6,2)-D (HA-CA-CO)-N- HN	24	[123]
Sidechain assignments	Nck Sh3-1	(4,3)-D HC(CO)NH- TOCSY, with nonuniform sampling and MaxEnt reconstruction in both the combined HC dimension and the conventional N dimension	48	[127]
Membrane protein backbone And sidechain assignments	Subunit c of F₁F₀ ATP synthase in micelles	previously published (3,2)- D HNNCO; (4,3)-D L- HNC^α/βC^α, L-HN(CO)C^α/βC^α HCCH; (4,2)-D HACA(CO)NH; (5,3)-D intra-HN{<N,CO>}{C^α/βC^α} and {C^α/βC^α}{CON}NH	118	[132]
Scalar coupling constants	9.5 kDa M-crystallin 16.2 kDa Eh-CaBP	(3,2)-D quantitative-J HNHA, HNHB	1.5 to 18	[133]
Pseudocontact shifts	8.5 kDa calbindin	previously published (3,2)- D HNCO, HN(CO)CA, HN(COCA)CB, HNHA	7.5	[134]
NOE-derived distance restraints	1.4 mM ubiquitin	(4,3)-D time-shared NOESY detecting HN CH and HN NH	48	[126]

^†

(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 independen 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. intra- indicates that only the intraresidue peaks are detected. [Square brackets] indicate time-shared evolution of two nuclei, with diagonal slashes separating the nuclei or sets of nuclei that evolve independently. L- indicates that longitudinal relaxation optimization is used. Hyphens between nuclei indicate that the coupling between the nuclei are evolved. The names for some experiments have been adjusted from the original publications to maintain consistency in nomenclature.

^‡

The measurement times represent the time reported for running the set of experiments on the sample, or a range of times for multiple samples. Where multiple individual times are listed on separate lines, they correspond to the samples listed in the sample column, and are in the same order. For the YqfB structure determination, a+b indicates a hours for the assignment experiments and b hours for the NOESY.