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1H, 15N, 13C resonance assignment of folded and 8 M urea-denatured state of SUMO from Drosophila melanogaster
- Dinesh Kumar, Ashutosh Kumar, Jyoti R. Misra, Jeetender Chugh, Shilpy Sharma, R. Hosur
- BiologyBiomolecular NMR assignments
- 1 June 2008
NMR resonance assignment of the folded and 8 M urea-denatured state of SUMO from Drosophila melanogaster (dsmt3) is reported.
Tuning the HNN experiment: generation of serine–threonine check points
The tunability of the HNN experiment is described to obtain certain residue specific peak patterns in the spectra of (15N, 13C) labeled proteins by tuning a band-selective 180° pulse on the carbon channel in the pulse sequence, whereby one can tamper with the Cα–Cβ coupling evolutions for the different residues.
hNCOcanH pulse sequence and a robust protocol for rapid and unambiguous assignment of backbone (1HN, 15N and 13C′) resonances in 15 N/13C‐labeled proteins
The hNCOcanH experiment in combination with the HNN experiment described previously leads to a more robust assignment protocol for backbone resonances (1HN, 15N) than could be derived from the combination of HNN and HN(C)N experiments.
BEST-HNN and 2D-(HN)NH experiments for rapid backbone assignment in proteins.
(15N ± 13C′) edited (4, 3)D‐H(CC)CONH TOCSY and (4, 3)D‐NOESY HNCO experiments for unambiguous side chain and NOE assignments of proteins with high shift degeneracy
These reduced dimensionality experiments in combination with routinely used 15N and 13C′ edited TOCSY and NOESY experiments will provide an alternative way for high‐quality NMR structure determination of large unstable proteins (with very high shift degeneracy), which are not at all amenable to 4D NMR.
Conserved structural and dynamics features in the denatured states of drosophila SUMO, human SUMO and ubiquitin proteins: Implications to sequence‐folding paradigm
The various results suggest that hydrophobic clusters as well as different native and non‐native secondary structural elements are transiently formed in urea‐denatured state of dSmt3.
hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment in (13C, 15N) labeled proteins.
AUTOBA: Automation of backbone assignment from HN(C)N suite of experiments
An efficient algorithm named as AUTOBA (Automatic Backbone Assignment) designed to automate the assignment protocol based on HN(C)N suite of experiments, demonstrated with experimental spectra recorded on two small globular proteins and simulated spectra of 27 other proteins using assignment data from the BMRB.
Direct Sequential Hit Strategy for Unambiguous and Accurate Backbone Assignment of 13C/15N Labeled Proteins
An efficient strategy -named here as strategy— has been presented for unambiguous and accurate backbone assignment of 13C/15N labeled proteins using an intrinsically unfolded 164-residue protein named DLC1 binding domain of nNOS.