Auto-encoding NMR chemical shifts from their native vector space to a residue-level biophysical index

Protein structure determination from NMR chemical shifts.

NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural c...

H Chemical Shifts in NMR

Sensitivity Encoding of Chemical Shifts

INTRODUCTION The chemical shift artifact (CSA) results from temporally undersampling a spatial-spectral distribution along a tilted k-t trajectory. This is illustrated in Fig. 1 for the case of H imaging. Figure 1(a) shows a typical H spatial-spectral distribution, in which the two predominant spectral components are from lipid and water protons. Figure 1(b) shows the k-t space sampling pattern...

SimShift: Identifying structural similarities from NMR chemical shifts

MOTIVATION An important quantity that arises in NMR spectroscopy experiments is the chemical shift. The interpretation of these data is mostly done by human experts; to our knowledge there are no algorithms that predict protein structure from chemical shift sequences alone. One approach to facilitate this process could be to compare two such sequences, where the structure of one protein has alr...

NMR chemical shifts in periodic systems from first principles

A recently developed ab-initio method for the calculation of NMR chemical shifts and magnetic susceptibilities in systems under periodic boundary conditions is presented and applied to a hydrogen-bonded molecular crystal. The calculations can unambiguously assign the chemical shifts to individual atoms in experimental spectra, and can further serve for the validation of simulated atomic traject...