Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules.
Chemical-shift-selective (13C, 13C) polarization transfer is analyzed in uniformly labeled biomolecules. It is shown that the spin system dynamics remain sensitive to the distance of interest and can be well reproduced within a quantum-mechanical multiple-spin analysis. These results lead to a general approach on how to describe chemical-shift-selective transfer in uniformly labeled systems. As demonstrated in the case of ubiquitin, this methodology can be used to detect long-range distance constraints in uniformly labeled proteins.
Sonnenberg
Lars
L
Department for NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Luca
Sorin
S
Baldus
Marc
M
D001704:Biopolymers / Q000032:analysis / Q000737:chemistry*; D002247:Carbon Isotopes; D003198:Computer Simulation; D003461:Crystallography / Q000379:methods*; D006639:Histidine / Q000032:analysis / Q000737:chemistry*; D006851:Hydrochloric Acid / Q000032:analysis / Q000737:chemistry; D007553:Isotope Labeling / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D013113:Spin Labels; D025801:Ubiquitin / Q000032:analysis / Q000737:chemistry*
D001704:Biopolymers; D002247:Carbon Isotopes; D013113:Spin Labels; D025801:Ubiquitin; D006639:Histidine; D006851:Hydrochloric Acid