Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules

Abstract

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.

High‐Resolution Solid‐State NMR Structure of an Anticancer Agent

“…To obtain a similarly large constraint set with solid-state NMR spectroscopic methods that rely on the detection of individual 13 C-13 C distances, [40][41][42] a build-up of two-dimensional experiments would have to be performed for each distance. Even though the CHHC experiment involves three CP transfer steps and is thus less sensitive than chemical shift selective transfer methods, which involve only one CP, the total time needed to obtain the 3D structure is drastically reduced.…”

Effective dipolar couplings determined by dipolar dephasing of double-quantum coherences

“…The effective dipolar coupling as defined in Eq. (15) is an approximation for the initial part of the DQ dephasing curve in multiple spin systems and needs to be validated against experimental evidence. In Fig.…”

“…Some of these methods have already been applied to multiple-spin systems [11][12][13][14][15]. A rather successful subclass of experiments are doublequantum (DQ) filtered experiments which can be used to encode the dipolar interaction either by rotor phase modulation [16,17] or by varying the double-quantum/zeroquantum conversion times [18,19].…”

NMR spectroscopy of basic/aromatic amino acid clusters in membrane proteins

“…These methods have been reviewed [124][125][126]. For example, Ramamoorthy and co-workers [52] have described 13 C-15 N rotational echo double-resonance experiments in multilamellar vesicles to establish the helical conformation of the C-terminal segment of paradaxin Pa4 in lipid membranes.…”