Characterization of protein secondary structure from NMR chemical shifts

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...

Interleukin-1 Receptor Antagonist Protein: Solution Secondary Structure from NOE's and 1H« and 13C« Chemical Shifts

Inter leukinla and interleukin-ip are two polypeptides which share a significant number of inflammatory, immunological and pathological properties (for a review see [1]). Importantly, these dissimilar 17 kDa proteins bind to two classes of interleukin-1 receptors, resulting in the mediation of several immune and inflammatory responses and in the induction of a variety of biological changes in n...

Correlation between 15N NMR chemical shifts in proteins and secondary structure.

An empirical correlation between the peptide 15N chemical shift, delta 15Ni, and the backbone torsion angles phi i, psi i-1 is reported. By using two-dimensional shielding surfaces delta (phi i, psi i-1), it is possible in many cases to make reasonably accurate predictions of 15N chemical shifts for a given structure. On average, the rms error between experiment and prediction is about 3.5 ppm....

Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach.

Recent theoretical developments permit the prediction of 1H, 13C, 15N, and 19F nuclear magnetic resonance chemical shifts in proteins and offer new ways of analyzing secondary and tertiary structure as well as for probing protein electrostatics. For 13C, phi, psi torsion angles dominate shielding for C alpha and C beta, but the addition of hydrogen bonding and electrostatics gives even better a...

H Chemical Shifts in NMR