Abstract
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids. Such biological samples feature functionally relevant molecular dynamics, which often affect different parts of the sample in different ways. Solid-state NMR experiments’ sensitivity to dynamics represents a double-edged sword. On the one hand, it offers a chance to measure dynamics in great detail. On the other hand, certain types of motion lead to signal loss and experimental inefficiencies that at first glance interfere with the application of ssNMR to overly dynamic proteins. Dynamics-based spectral editing (DYSE) ssNMR methods leverage motion-dependent signal losses to simplify spectra and enable the study of sub-structures with particular motional properties.
| Original language | English |
|---|---|
| Pages (from-to) | 123-135 |
| Number of pages | 13 |
| Journal | Methods |
| Volume | 148 |
| DOIs | |
| State | Published - 15 Sep 2018 |
| Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2018 The Authors
Funding
This work was supported by the National Institutes of Health R01 AG019322 , R01 GM112678 , R01 GM113908 , and S10 grant OD012213-01 . The authors acknowledge fruitful discussions with past and current members of the Van der Wel research group.
| Funders | Funder number |
|---|---|
| National Institutes of Health | OD012213-01, R01 GM113908, R01 AG019322 |
| National Institute of General Medical Sciences | R01GM112678 |
Keywords
- Dynamics
- Membrane proteins
- Protein aggregation
- Solid-state NMR
- Structural biology