Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus.
The majority of proteins exist in vivo within macromolecular assemblies whose functions are dependent on dynamical processes spanning a wide range of time scales. One such assembly is formed by the molecular chaperone αB-crystallin that exists in a variety of exchanging oligomeric states, centred on...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2011
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