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Article Abstract
To study the structure and dynamics of proteins by nuclear magnetic resonance (NMR), sequence-specific assignment is needed, which can be obtained by acquiring and analyzing multiple triple-resonance experiments with the three-dimensional TROSY-HNCA, the most sensitive stand-alone experiment with which sequential assignment is, in principle, possible. However, gaining an unambiguous assignment solely from this spectrum is generally not possible because amino acid-type information cannot be gleaned only from the C shifts and the low resolution in the C dimension, which is limited by the homonuclear coupling of the C and C nuclei. Here, super-resolution NMR is applied to the TROSY-HNCA and HNcoCA experiments, yielding pseudo-decoupling, which results in a four- to fivefold resolution enhancement in the C dimension, essential for the assignment, which allows for straightforward assignment of proteins as large as 500 residues based on simulations.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12356247 | PMC |
| http://dx.doi.org/10.1126/sciadv.adv6246 | DOI Listing |
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