NDLI: Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag

Content Provider	Springer Nature Link
Author	Sengupta, Ishita Gao, Min Arachchige, Rajith J. Nadaud, Philippe S. Cunningham, Timothy F. Saxena, Sunil Schwieters, Charles D. Jaroniec, Christopher P.
Copyright Year	2014
Abstract	Paramagnetic relaxation enhancements (PREs) are a rich source of structural information in protein solid-state NMR spectroscopy. Here we demonstrate that PRE measurements in natively diamagnetic proteins are facilitated by a thiol-reactive compact, cyclen-based, high-affinity Cu$^{2+}$ binding tag, 1-[2-(pyridin-2-yldisulfanyl)ethyl]-1,4,7,10-tetraazacyclododecane (TETAC), that overcomes the key shortcomings associated with the use of larger, more flexible metal-binding tags. Using the TETAC–Cu$^{2+}$ K28C mutant of B1 immunoglobulin-binding domain of protein G as a model, we find that amino acid residues located within ~10 Å of the Cu$^{2+}$ center experience considerable transverse PREs leading to severely attenuated resonances in 2D $^{15}$N–$^{13}$C correlation spectra. For more distant residues, electron–nucleus distances are accessible via quantitative measurements of longitudinal PREs, and we demonstrate such measurements for $^{15}$N–Cu$^{2+}$ distances up to ~20 Å.
Starting Page	1
Ending Page	6
Page Count	6
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	61
Issue Number	1
e-ISSN	15735001
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-11-29
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Solid-state NMR Magic-angle spinning Paramagnetic relaxation Metal binding tag Protein structure Biophysics and Biological Physics Biochemistry Spectroscopy/Spectrometry
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

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Protein Structural Studies by Paramagnetic Solid-State NMR Spectroscopy Aided by a Compact Cyclen-Type Cu(II) Binding Tag

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