AI Article Synopsis
- The authors introduce 2D spectroscopy methods derived from popular 3D and 4D experiments used for protein resonance assignments, focusing on HN(CO) CACB and similar techniques.
- These 2D experiments allow researchers to gather information about connections between amino proton and nitrogen shifts as well as carbon shifts within protein residues.
- Although slightly less sensitive than their 3D counterparts, these 2D spectra are useful for automated assignments and accelerate the structural analysis of small to medium-sized proteins in structural genomics.
Article Abstract
We present 2D versions of the popular triple resonance HN(CO) CACB, HN(COCA)CACB, HN(CO)CAHA, and HN(COCA) CAHA experiments, commonly used for sequential resonance assignments of proteins. These experiments provide information about correlations between amino proton and nitrogen chemical shifts and the alpha- and beta-carbon and alpha-proton chemical shifts within and between amino acid residues. Using these 2D spectra, sequential resonance assignments of H(N), N, C(alpha), C(beta), and H(alpha) nuclei are easily achieved. The resolution of these spectra is identical to the well-resolved 2D (15)N-(1)H HSQC and H(NCO)CA spectra, with slightly reduced sensitivity compared to their 3D and 4D versions. These types of spectra are ideally suited for exploitation in automated assignment procedures and thereby constitute a fast and efficient means for NMR structural determination of small and medium-sized proteins in solution in structural genomics programs.
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| http://dx.doi.org/10.1006/jmre.2002.2537 | DOI Listing |
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