Unknown

Dataset Information

0

Optimal control theory enables homonuclear decoupling without Bloch-Siegert shifts in NMR spectroscopy.


ABSTRACT: The Bloch-Siegert shift is a phenomenon in NMR spectroscopy and atomic physics in which the observed resonance frequency is changed by the presence of an off-resonance applied field. In NMR, it occurs especially in the context of homonuclear decoupling. Here we develop a practical method for homonuclear decoupling that avoids inducing Bloch-Siegert shifts. This approach enables accurate observation of the resonance frequencies of decoupled nuclear spins. We apply this method to increase the resolution of the HNCA experiment. We also observe a doubling in sensitivity for a 30?kDa protein. We demonstrate the use of band-selective C? decoupling to produce amino acid-specific line shapes, which are valuable for assigning resonances to the protein sequence. Finally, we assign the backbone of a 30?kDa protein, Human Carbonic Anhydrase II, using only HNCA experiments acquired with band-selective decoupling schemes, and instrument time of one week.

SUBMITTER: Coote PW 

PROVIDER: S-EPMC6070575 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC3790959 | biostudies-literature
| S-EPMC4017862 | biostudies-literature
| S-EPMC7187420 | biostudies-literature
| S-EPMC8317164 | biostudies-literature
| S-EPMC6771691 | biostudies-literature
| S-EPMC5076794 | biostudies-literature
| S-EPMC3669656 | biostudies-other
| S-EPMC5396389 | biostudies-literature
| S-EPMC7426724 | biostudies-literature
| S-EPMC6040279 | biostudies-literature