Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy
In structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic dist...
| Main Author: | |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2021-12-01
|
| Series: | Frontiers in Molecular Biosciences |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2021.791090/full |
| _version_ | 1818983205909299200 |
|---|---|
| author | Patrick C. A. van der Wel |
| author_facet | Patrick C. A. van der Wel |
| author_sort | Patrick C. A. van der Wel |
| collection | DOAJ |
| description | In structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic distance measurements. In the current review, we examine the utility of ssNMR measurements of angular constraints, as a complement to distance-based structure determination. The focus is on direct measurements of angular restraints via the judicious recoupling of multiple anisotropic ssNMR parameters, such as dipolar couplings and chemical shift anisotropies. Recent applications are highlighted, with a focus on studies of nanocrystalline polypeptides, aggregated peptides and proteins, receptor-substrate interactions, and small molecule interactions with amyloid protein fibrils. The review also examines considerations of when and where ssNMR torsion angle experiments are (most) effective, and discusses challenges and opportunities for future applications. |
| first_indexed | 2024-12-20T17:59:25Z |
| format | Article |
| id | doaj.art-d02fd834872d4a0dbf996de7a85135ff |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-20T17:59:25Z |
| publishDate | 2021-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-d02fd834872d4a0dbf996de7a85135ff2022-12-21T19:30:40ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2021-12-01810.3389/fmolb.2021.791090791090Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR SpectroscopyPatrick C. A. van der WelIn structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic distance measurements. In the current review, we examine the utility of ssNMR measurements of angular constraints, as a complement to distance-based structure determination. The focus is on direct measurements of angular restraints via the judicious recoupling of multiple anisotropic ssNMR parameters, such as dipolar couplings and chemical shift anisotropies. Recent applications are highlighted, with a focus on studies of nanocrystalline polypeptides, aggregated peptides and proteins, receptor-substrate interactions, and small molecule interactions with amyloid protein fibrils. The review also examines considerations of when and where ssNMR torsion angle experiments are (most) effective, and discusses challenges and opportunities for future applications.https://www.frontiersin.org/articles/10.3389/fmolb.2021.791090/fullsolid-state NMRstructural biologyamyloidpolyglutamineprotein structures |
| spellingShingle | Patrick C. A. van der Wel Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy Frontiers in Molecular Biosciences solid-state NMR structural biology amyloid polyglutamine protein structures |
| title | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy |
| title_full | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy |
| title_fullStr | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy |
| title_full_unstemmed | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy |
| title_short | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy |
| title_sort | dihedral angle measurements for structure determination by biomolecular solid state nmr spectroscopy |
| topic | solid-state NMR structural biology amyloid polyglutamine protein structures |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2021.791090/full |
| work_keys_str_mv | AT patrickcavanderwel dihedralanglemeasurementsforstructuredeterminationbybiomolecularsolidstatenmrspectroscopy |