| Autor: |
Kwan TOC; National Physical Laboratory, Teddington, UK.; Research Complex at Harwell Rutherford, Appleton Laboratory, Oxford, UK., Reis R; National Physical Laboratory, Teddington, UK.; Research Complex at Harwell Rutherford, Appleton Laboratory, Oxford, UK., Moraes I; National Physical Laboratory, Teddington, UK. isabel.moraes@npl.co.uk.; Research Complex at Harwell Rutherford, Appleton Laboratory, Oxford, UK. isabel.moraes@npl.co.uk. |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2021; Vol. 2208, pp. 189-202. |
| DOI: |
10.1007/978-1-0716-0928-6_13 |
| Abstrakt: |
Integral membrane proteins are important drug targets that are critical in supporting many biological processes. Despite that, the study of their structure-function relationships remains a major goal in structural biology, yet progress has been hampered by inherent challenges in the production for stable and homogeneous protein samples. Dynamic light scattering provides a straightforward probe of protein quality in solution, particularly in relation to stability and aggregation. However, the necessity to use large amounts of sample and the low-throughput nature of the analysis remain as major bottlenecks of the technique.Here, we present a protocol for dynamic light scattering measurements that are executed in a fully automated fashion for low-volume samples, in situ. The protocol offers a generic pre-screening method for downstream structural studies of biomolecules using higher-resolution approaches such as X-ray crystallography, electron microscopy, small-angle X-ray scattering, and NMR . |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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