Abstract
The essential pathway by which light-harvesting chlorophyll binding proteins are inserted into the thylakoid of the chloroplast is mediated by a unique signal recognition particle (cpSRP). Its novel 43kDa subunit (cpSRP43) contains three chromodomains (CDs). CD2 has been shown to be significant in various aspects of the cpSRP-mediated pathway. While structural information about CD2 is known, this study aims to gain a more comprehensive understanding of the structural stability through analysis of hydrogen-deuterium exchange. 15N-labeled CD2 samples will be produced from over-expression of CD2 in E. coli cultured in labeled media. Subsequently, the readily-occurring exchange between amide hydrogen and solvent deuterium will be monitored by NMR spectroscopy. The kinetics of the exchange can provide useful information about the free energy of exchange and thus the stability.
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