[NMR paper] Efficient and accurate determination of 13C T1 and T1? relaxation time constants of high-mobility polymers from limited-resolution spectra with optimized pulse sequences and data fitting
Efficient and accurate determination of 13C T1 and T1? relaxation time constants of high-mobility polymers from limited-resolution spectra with optimized pulse sequences and data fitting
The pulse sequences for the measurement of 13C T1 and T1? relaxation time constants in soft organic solids were modified to include steady-state nuclear Overhauser enhancement with direct polarization (ssNOE/DP). The increased signal intensities with ssNOE are particularly well-suited for highly mobile and structurally heterogeneous polymers and proteins like elastin. The phase cycling of these experiments was modified to yield datasets that require less time, with more accurate results. The “3D-fitting process” was developed and then optimized for natural-abundance 13C spectra of elastin, with its characteristic and significant overlap. A comparison of 3D-fitting with the similarly purposed SPORT (Geppi and Forte, 1999) illustrates that the former is more robust, with smaller uncertainty values and higher precision.
Accurate determination of rates from non-uniformly sampled relaxation data
Accurate determination of rates from non-uniformly sampled relaxation data
Abstract
The application of non-uniform sampling (NUS) to relaxation experiments traditionally used to characterize the fast internal motion of proteins is quantitatively examined. Experimentally acquired Poisson-gap sampled data reconstructed with iterative soft thresholding are compared to regular sequentially sampled (RSS) data. Using ubiquitin as a model system, it is shown that 25Â*% sampling is sufficient for the determination of quantitatively accurate relaxation...
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Accurate measurement of 3 J HNHα couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra
Accurate measurement of 3 J HNHα couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra
Abstract
Provided that care is taken in adjusting the WATERGATE element of a 1Hâ??15N TROSY-HSQC experiment, such that neither the water magnetization nor the 1Hα protons are inverted by its final 180° pulse, 3JHNHα couplings can be measured directly from splittings in the 1H dimension of the spectrum. With band-selective 1H decoupling, very high 15N resolution can be achieved. A complete set of 3JHNHα values, ranging from 3.4 to...
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[NMR paper] Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity-Optimized NMR Pulse Sequences.
Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity-Optimized NMR Pulse Sequences.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity-Optimized NMR Pulse Sequences.
Angew Chem Int Ed Engl. 2013 Aug 14;
Authors: Dallmann A, Simon B, Duszczyk MM, Kooshapur H, Pardi A, Bermel W, Sattler M
Abstract
Improved Sensitivity:...
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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[NMR paper] Determination of protein rotational correlation time from NMR relaxation data at vari
Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
Related Articles Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
J Biomol NMR. 2004 Dec;30(4):431-42
Authors: Korchuganov DS, Gagnidze IE, Tkach EN, Schulga AA, Kirpichnikov MP, Arseniev AS
An accurate determination of the overall rotation of a protein plays a crucial role in the investigation of its internal motions by NMR. In the present work, an innovative approach to the...
Efficient and accurate determination of 13C T1 and T1? relaxation time constants of high-mobility polymers from limited-resolution spectra with optimized pulse sequences and data fitting
Linear Mode
