The NMR sample was supplied with 5% (v/v) D2O. All NMR spectra were acquired at 298 K on a Bruker 800 MHz AVANCE III spectrometer. Data were processed using NMRPipe (Delaglio et al. 1995) software and analyzed with CCPNMR Analysis (Vranken et al. 2005). Backbone resonance assignments were determined using the 15N–1H-HSQC spectrum (Fig. 1) together with a set of triple resonance experiments: HNCO, HN(CA)CO, HNCA, CBCA(CO)NH, HNCACB, and HBHA(CO)NH. Side-chain resonance assignments were performed using 13C-HSQC, (H)CCH-TOCSY, HCCH-TOCSY, and 15N and 13C-NOESY-HSQC experiments. The chemical shift of water proton was used as an internal reference for 1H while 13C and 15N chemical shifts were referenced indirectly to water (Wishart et al. 1995).

15N–1H-HSQC spectrum of the N-terminal domain (residues 56 to 193) of the nucleocapsid protein of hCoV-HKU1. Peak assignments are indicated by residue number and the one-letter amino acid code

Note: The content above has been extracted from a research article, so it may not display correctly.



Q&A
Please log in to submit your questions online.
Your question will be posted on the Bio-101 website. We will send your questions to the authors of this protocol and Bio-protocol community members who are experienced with this method. you will be informed using the email address associated with your Bio-protocol account.



We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.