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Redox- and metal-directed structural diversification in designed metalloprotein assemblies
Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown - through extensive structural and biophysical characterization - to access five distinc...
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| Published in: | Chemical communications (Cambridge, England) England), 2022-06, Vol.58 (49), p.6958-6961 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c370c-94195dc7acd23b04bd6a732965c91b2b3a6deb03ad0b58ab479c69f5142b00c93 |
| container_end_page | 6961 |
| container_issue | 49 |
| container_start_page | 6958 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 58 |
| creator | Kakkis, Albert Golub, Eyal Choi, Tae Su Tezcan, F. Akif |
| description | Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown - through extensive structural and biophysical characterization - to access five distinct oligomeric states, exemplifying how the complex interplay between hydrophobic, metal-ligand, and reversible covalent interactions could be harnessed to obtain multiple, responsive protein architectures from a single building block.
Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. |
| doi_str_mv | 10.1039/d2cc02440c |
| format | article |
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| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2022-06, Vol.58 (49), p.6958-6961 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_crossref_primary_10_1039_D2CC02440C |
| source | Royal Society of Chemistry |
| subjects | Chemistry Coordination compounds Hydrophobic and Hydrophilic Interactions Ligands Metalloproteins - chemistry Metals - chemistry Oxidation-Reduction Proteins Self-assembly Structural analysis |
| title | Redox- and metal-directed structural diversification in designed metalloprotein assemblies |
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