Research output: Contribution to Journal/Magazine › Journal article › peer-review
<mark>Journal publication date</mark> | 7/03/2011 |
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<mark>Journal</mark> | Methods in Molecular Biology |
Volume | 684 |
Number of pages | 8 |
Pages (from-to) | 375-382 |
Publication Status | Published |
<mark>Original language</mark> | English |
Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites, thereby restoring the sites to catalytic competence. This chapter reports methods developed for assaying the two activities of Rubisco activase: ATP hydrolysis and Rubisco activation.