3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins |
| |
Authors: | Thomas Szyperski Gerhard Wider John H Bushweller Kurt Wüthrich |
| |
Institution: | (1) Eidgenössische Technische Hochschule-Hönggerberg, Institut für Molekularbiologie und Biophysik, CH-8093 Zürich, Switzerland |
| |
Abstract: | Summary The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HACAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses 13C –15N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the 13C and 15N nuclei, thereby providing the four resonance frequencies of the -proton, the -carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in 13C-15N-double-labeled proteins.Abbreviations 3D, 4D
three-dimensional, four-dimensional
- TPPI
time-proportional phase incrementation
- ct
constant-time
- rf
radiofrequency
- NOE
nuclear Overhauser enhancement
- NOESY
two-dimensional nuclear Overhauser enhancement spectroscopy
- glutaredoxin(C14S)
mutant E. coli glutaredoxin with the cysteine at position 14 replaced by serine |
| |
Keywords: | NMR Resonance assignments Heteronuclear two-spin coherence spectroscopy Protein structure determination |
本文献已被 SpringerLink 等数据库收录! |
|