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
Assignment of NMR spectra of proteins using triple-resonance two-dimensional experiments
β Scribed by Jean-Pierre Simorre; Bernhard Brutscher; Michael S. Caffrey; Dominique Marion
- Publisher
- Springer Netherlands
- Year
- 1994
- Tongue
- English
- Weight
- 632 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0925-2738
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β¦ Synopsis
Two-dimensional versions of HNCA and HNCO experiments are described, which provide essentially the same information as the 3D sequence. A multiple-quantum coherence involving either lSN and 13C~ or 15N and 13CO is created. One of the two frequencies is given by the middle point between the two cross peaks (zero-and double-quantum) and the other by their separation. Quadrature detection can be performed on either nucleus, modifying only the appearence of the 2D spectrum, but not the information content. These experiments, named MQ-HNCA and MQ-HNCO, are illustrated on a (15N,13C) doubly labelled cytochrome c2 from Rhodobacter capsulatus (116 amino acids).
π SIMILAR VOLUMES
## Abstract A complete assignment of all resonances of a small organic molecule is a prerequisite for a structure determination using NMR spectroscopy. This is conventionally obtained using a wellβestablished strategy based on COSY, HMQC and HMBC spectra. In case of phycocyanobilin (PCB) in HMPT th