TROSY-based correlation and NOE spectroscopy for NMR structural studies of large proteins.

Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Transverse relaxation-optimized spectroscopy (TROSY) is based on the fact that cross-correlation relaxation rates associated with the interferences between chemical shift anisotropy and dipole-dipole interactions can be dramatically reduced. TROSY selects these slowly relaxing components of 15N-1HN or 13C-1H antiphase coherences to significantly enhanced signal sensitivity and spectral resolution for large proteins (>30 kD). The basic principles and applications of three- and four-dimensional TROSY-based triple-resonance experiments and NOESY experiments for structure-function studies of proteins are discussed in this chapter. To make applications of these experiments easier, some of the experimental setups are also described.

Original languageEnglish (US)
Pages (from-to)57-78
Number of pages22
JournalMethods in molecular biology (Clifton, N.J.)
Volume278
StatePublished - Oct 11 2004

Fingerprint Dive into the research topics of 'TROSY-based correlation and NOE spectroscopy for NMR structural studies of large proteins.'. Together they form a unique fingerprint.

Cite this