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Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

ABSTRACT: Chemical shift tensors (CSTs) are an exquisite probe of local geometric and electronic structure. 15N CST are very sensitive to hydrogen bonding, yet they have been reported for very few proteins to date. Here we present experimental results and statistical analysis of backbone amide 15N CSTs for 100 residues of four proteins, two E. coli thioredoxin reassemblies (1-73-(U-13C,15N)/74-108-(U-15N) and 1-73-(U-15N)/74-108-(U-13C,15N)), dynein light chain 8 LC8, and CAP-Gly domain of the mammalian dynactin. The 15N CSTs were measured by a symmetry-based CSA recoupling method, ROCSA. Our results show that the principal component ?11 is very sensitive to the presence of hydrogen bonding interactions due to its unique orientation in the molecular frame. The downfield chemical shift change of backbone amide nitrogen nuclei with increasing hydrogen bond strength is manifested in the negative correlation of the principal components with hydrogen bond distance for both ?-helical and ?-sheet secondary structure elements. Our findings highlight the potential for the use of 15N CSTs in protein structure refinement.

SUBMITTER: Paramasivam S

PROVIDER: S-EPMC6261280 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

Paramasivam Sivakumar S Gronenborn Angela M AM Polenova Tatyana T

Solid state nuclear magnetic resonance 20180315

Chemical shift tensors (CSTs) are an exquisite probe of local geometric and electronic structure. 15N CST are very sensitive to hydrogen bonding, yet they have been reported for very few proteins to date. Here we present experimental results and statistical analysis of backbone amide 15N CSTs for 100 residues of four proteins, two E. coli thioredoxin reassemblies (1-73-(U-13C,15N)/74-108-(U-15N) and 1-73-(U-15N)/74-108-(U-13< ...[more]

PMID: 29579703

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Project description:(13)C and (15)N chemical shift (CS) interaction is a sensitive probe of structure and dynamics in a wide variety of biological and inorganic systems, and in the recent years several magic angle spinning NMR approaches have emerged for residue-specific measurements of chemical shift anisotropy (CSA) tensors in uniformly and sparsely enriched proteins. All of the currently existing methods are applicable to slow and moderate magic angle spinning (MAS) regime, i.e., MAS frequencies below 20 kHz. With the advent of fast and ultrafast MAS probes capable of spinning frequencies of 40-100 kHz, and with the superior resolution and sensitivity attained at such high frequencies, development of CSA recoupling techniques working under such conditions is necessary. In this work, we present a family of R-symmetry based pulse sequences for recoupling of (13)C∕(15)N CSA interactions that work well in both natural abundance and isotopically enriched systems. We demonstrate that efficient recoupling of either first-rank (σ(1)) or second-rank (σ(2)) spatial components of CSA interaction is attained with appropriately chosen γ-encoded RN(n)(v) symmetry sequences. The advantage of these γ-encoded RN(n)(v)-symmetry based CSA (RNCSA) recoupling schemes is that they are suitable for CSA recoupling under a wide range of MAS frequencies, including fast MAS regime. Comprehensive analysis of the recoupling properties of these RN(n)(v) symmetry sequences reveals that the σ(1)-CSA recoupling symmetry sequences exhibit large scaling factors; however, the partial homonuclear dipolar Hamiltonian components are symmetry allowed, which makes this family of sequences suitable for CSA measurements in systems with weak homonuclear dipolar interactions. On the other hand, the γ-encoded symmetry sequences for σ(2)-CSA recoupling have smaller scaling factors but they efficiently suppress the homonuclear dipole-dipole interactions. Therefore, the latter family of sequences is applicable for measurements of CSA parameters in systems with strong homonuclear dipolar couplings, such as uniformly-(13)C labeled biological solids. We demonstrate RNCSA NMR experiments and numerical simulations establishing the utility of this approach to the measurements of (13)C and (15)N CSA parameters in model compounds, [(15)N]-N-acetyl-valine (NAV), [U-(13)C, (15)N]-alanine, [U-(13)C,(15)N]-histidine, and present the application of this approach to [U-(13)C∕(15)N]-Tyr labeled C-terminal domain of HIV-1 CA protein.

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Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

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Backbone amide <sup>15</sup>N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

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Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

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Backbone amide &lt;sup&gt;15&lt;/sup&gt;N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

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OmicsDI is part of the ELIXIR infrastructure

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Backbone amide <sup>15</sup>N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.