Protein Side-Chain Rotamers from Dipolar Couplings in a Liquid Crystalline Phase

Chou, James J.; Bax, Ad

doi:10.1021/ja015660y

Cited by 41 publications

(35 citation statements)

References 19 publications

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“…[7,8] Although RDCs have been routinely measured between covalently bound spins of fixed internuclear distance, long-range RDCs also provide potentially very powerful structural information. [9,10] It has been shown that measurement of 1 H-1 H RDCs can be made to high levels of precision in highly deuterated proteins, where dipolar truncation effects are avoided. The aim of this study is to determine, de novo, the backbone structure of perdeuterated protein GB1 in solution to the highest possible precision using only RDCs and residual 13 C' NMR chemical shifts (RCSs) measured in two different alignment media.…”

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confidence: 99%

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

et al. 2006

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NMR dipolar couplings can be measured for weakly aligned proteins and are sensitive probes of their structure and dynamics. The combination of fixed geometry and 1H–1H couplings alone from two alignment media provides access to ultrahigh‐resolution structures. The apparent precision, as measured by independent cross‐validation and structure comparison, is comparable to that available from high‐resolution X‐ray crystallography.

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confidence: 99%

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

et al. 2006

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“…The HNCO E.COSY method 2 in water (in phage) was recorded using two (four) transients with 80 (100), 96 (112) and 576 (576) complex points, corresponding to acquisition times of 36.4 (45.5), 43.6 (46.7 ms) and 64 ms in 13 C 0 , 15 N and 1 H dimensions, respectively. Total experimental time was 17 (48) h, yielding an average S/N ratio 30 (25). The HNCO E.COSY method 4 was recorded using two transients with 72, 70, and 640 complex points, corresponding to acquisition times of 32.7, 31.8 and 64 ms in 13 C 0 , 15 N and 1 H dimensions (experimental time was 12 h, S/N D 70).…”

Section: Methodsmentioning

confidence: 99%

Simultaneous determination of one- and two-bond scalar and residual dipolar couplings between¹³C′,¹³C^αand¹⁵N spins in proteins

2006

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Four simple and sensitive HNCO-based methods for measurement of 1J(C'Calpha), 1J(NCalpha) and 2J(NCalpha) coupling constants in protein main chains are presented. Three of these experiments enable the simultaneous measurement of 1J(C'Calpha), 1J(NCalpha) and 2J(NCalpha) couplings. Exploitation of the E.COSY principle provides excellent dispersion of cross peaks in the resulting 3D spectra. The couplings can be retrieved with good accuracy from peak-to-peak separations. Karplus parameterizations are provided for 1J(NCalpha) and 2J(NCalpha), obtained from a nearly complete set of couplings of human ubiquitin. In addition, feasibility of the proposed methodology for measuring several residual dipolar couplings (RDCs) simultaneously is assessed.

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“…However, as the effect is active for a short period, it can be ignored without introducing large errors, as has been done in some other methods that use J-modulation to measure the 13 C-1 H couplings. [19,21] Finally, pulse imperfections can also contribute to the systematic error observed. In any case, the deviation observed using Eqn (4) for the determination of the couplings is quite small and has no consequences in the use of Cα -Hα RDCs in structure calculations.…”

Section: Measurement Of Couplings In Ubiquitinmentioning

confidence: 99%

Simultaneous measurement of NH and CαHα coupling constants in proteins

Pantoja-Uceda

Santoro

2009

Magnetic Reson in Chemistry

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We present a pulse sequence for the simultaneous measurement of N-H and Calpha-Halpha couplings in double-labeled proteins from 2D spectra. The proposed sequence, a modification of the HN(CO)CA experiment, combines the J-modulation method and the IPAP scheme. The couplings can be readily retrieved from a series of 2D (15)N-(1)H correlation spectra, differing in the time point at which a (1)H 180 degrees pulse is applied. This induces an intensity modulation of the (15)N-(1)H correlation peaks with the Calpha-Halpha coupling. The Calpha-Halpha coupling is then obtained by fitting the observed intensities to the modulation equation. The N-H coupling is measured in each member of the set from peak-to-peak separations in the IPAP subspectra. The pulse sequence is experimentally verified with a sample of (15)N/(13)C-enriched ubiquitin.

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Protein Side-Chain Rotamers from Dipolar Couplings in a Liquid Crystalline Phase

Cited by 41 publications

References 19 publications

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

Simultaneous determination of one- and two-bond scalar and residual dipolar couplings between¹³C′,¹³C^αand¹⁵N spins in proteins

Simultaneous measurement of NH and CαHα coupling constants in proteins

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Protein Side-Chain Rotamers from Dipolar Couplings in a Liquid Crystalline Phase

Cited by 41 publications

References 19 publications

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

Ultrahigh‐Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

Simultaneous determination of one- and two-bond scalar and residual dipolar couplings between13C′,13Cαand15N spins in proteins

Simultaneous measurement of NH and CαHα coupling constants in proteins

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Simultaneous determination of one- and two-bond scalar and residual dipolar couplings between¹³C′,¹³C^αand¹⁵N spins in proteins