Abstract
This chapter discusses methodological approaches for the synthesis and purification of hydrophobic peptides and proteins and strategies, which allow the assembly of larger membrane proteins. One important aspect of the chemical synthesis of membrane proteins in order to study their functional properties necessitates their refolding into lipid membranes or solubilization in detergents. Intensive research has been continuing on the mechanism of membrane protein folding. The chapter presents three illustrative examples of successful syntheses of membrane proteins. Diacylglycerol kinase (DAGK) is a homotrimeric membrane-embedded enzyme that catalyzes phosphorylation of diacylglycerol to form phosphatidic acid. The halobacterial transducer of rhodopsin (NpHtrII) forms a 2:2 complex with sensory rhodopsin (NpSRII). Light activation of this receptor leads to an activation of a downstream His kinase. In the third example, the power of the chemical synthesis of proteins is used for elucidation of cation specificity of the potassium channel KcsA.
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