Thiol-ene reaction: a versatile tool in site-specific labelling of proteins with chemically inert tags for paramagnetic NMR.
Site-specific tagging of proteins with paramagnetic lanthanides generates valuable long-range structure restraints for structural biology by NMR spectroscopy. We show that the thiol-ene addition reaction offers a powerful tool for tagging proteins in a chemically stable manner with very small lanthanide tags.
State-Key Laboratory of Elemento-organic Chemistry, Nankai University, Tianjin, 300071, China.
Qing-Feng
QF
Li
Yin
Y
Yang
Ansis
A
Maleckis
Gottfried
G
Otting
Xun-Cheng
XC
Su
D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007094:Imides / Q000737:chemistry; D028581:Lanthanoid Series Elements / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism
C490177:ArgR protein, E coli; D029968:Escherichia coli Proteins; D007094:Imides; D028581:Lanthanoid Series Elements; D011506:Proteins; D012097:Repressor Proteins; D013438:Sulfhydryl Compounds; D025801:Ubiquitin