TY - CHAP
T1 - NMR studies of large protein systems
AU - Tzeng, Shiou Ru
AU - Pai, Ming Tao
AU - Kalodimos, Charalampos G.
PY - 2012
Y1 - 2012
N2 - Over the recent years, there has been increased interest in applying NMR spectroscopy for the characterization of proteins and protein complexes of large molecular weight. The combination of multidimensional NMR, novel pulse sequences allowing for the selection of slowly relaxing coherence pathways, and the development of a range of labeling techniques has enabled high-resolution NMR analyses of supramolecular systems of even megadalton size. Here, we describe how NMR can be used to obtain structural information in large systems by using as an example the recent structure determination of SecA ATPase (204 kDa) in complex with a signal peptide.
AB - Over the recent years, there has been increased interest in applying NMR spectroscopy for the characterization of proteins and protein complexes of large molecular weight. The combination of multidimensional NMR, novel pulse sequences allowing for the selection of slowly relaxing coherence pathways, and the development of a range of labeling techniques has enabled high-resolution NMR analyses of supramolecular systems of even megadalton size. Here, we describe how NMR can be used to obtain structural information in large systems by using as an example the recent structure determination of SecA ATPase (204 kDa) in complex with a signal peptide.
KW - Macromolecular complex
KW - Molecular machinery
KW - Paramagnetic resonance enhancement
KW - Stable isotope labeling
UR - http://www.scopus.com/inward/record.url?scp=84855865582&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84855865582&partnerID=8YFLogxK
U2 - 10.1007/978-1-61779-480-3_8
DO - 10.1007/978-1-61779-480-3_8
M3 - Chapter
C2 - 22167672
AN - SCOPUS:84855865582
SN - 9781617794797
T3 - Methods in Molecular Biology
SP - 133
EP - 140
BT - Protein NMR Techniques
ER -