Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements.
The measurement of (13)C directed-detected paramagnetic relaxation enhancements (PREs) on spin-labeled proteins combines the efficacy of PREs for the detection of long-range distance information with the favorable sensitivity and resolution of (13)C direct-detected experiments. The (13)C PREs provide long-range distance restraints to map binding interfaces in proteins and protein complexes and are especially useful for studies of high-molecular weight perdeuterated molecules.
Madl
Tobias
T
Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
Felli
Isabella C
IC
Bertini
Ivano
I
Sattler
Michael
M
D002247:Carbon Isotopes / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D009687:Nuclear Proteins; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012261:Ribonucleoproteins; D013113:Spin Labels; D000072668:Splicing Factor U2AF
D002247:Carbon Isotopes; D009687:Nuclear Proteins; D011506:Proteins; D012261:Ribonucleoproteins; D013113:Spin Labels; D000072668:Splicing Factor U2AF