NDLI: Assignment Strategy for Fast Relaxing Signals: Complete Aminoacid Identification in Thulium Substituted Calbindin D$

Content Provider	Springer Nature Link
Author	Balayssac, Stéphane Jiménez, Beatriz Piccioli, Mario
Copyright Year	2006
Abstract	Paramagnetic proteins generally contain regions with diverse relaxation properties. Nuclei in regions far from the metal center may behave like those in diamagnetic proteins, but those closer to the metal experience rapid relaxation with accompanying line broadening. We have used a set of NMR experiments optimized to capture data from these various concentric regions in assigning the signals from a paramagnetic Calbindin D$_{9K}$ derivative in which one of the two calcium ions has been replaced by thulium(III). Normal double- and triple-resonance experiments with $^{1}$H detection were used in collecting data from nuclei in the diamagnetic-like region; these approaches identified signals from fewer than 50% of the amino acid residues (those with d>17.5 Å from thulium(III)). Paramagnetism-optimized two-dimensional NMR experiments with $^{1}$H detection were used in collecting data from nuclei in the next nearer region (d>15 Å). Standard (d>14 Å) and optimized (d>9 Å) $^{13}$C direct-detection experiments were used to capture data from nuclei in the next layer. Finally nuclei closest to the metal were detected by one-dimensional $^{13}$C (d>5 Å) and one-dimensional $^{15}$N data collection (d>4.2 Å). NMR signals were assigned on the basis of through-bond correlations and, for signals closest to the metal, pseudocontact shifts. The latter were determined from chemical shift differences between assigned signals in thulium(III) and lanthanum(III) derivatives of Calbindin D$_{9K}$ and they were interpreted on the basis of a structural model for the lanthanide-substituted protein. This approach yielded assignments of at least one resonance per amino acid residue, including those in the thulium(III) coordination sphere.
Starting Page	63
Ending Page	73
Page Count	11
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	34
Issue Number	2
e-ISSN	15735001
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2006-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	$^{13}$C & $^{15}$N direct detection NMR spectroscopy paramagnetic NMR pseudo-contact shifts sequence specific assignment solution structure determination Biochemistry Biophysics/Biomedical Physics Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

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