Strategies for the purification of membrane proteins
Citation:
Strategies for the purification of membrane proteins, Dermot Walls & Sinead Loughran, Methods in Molecular Biology, Springer, 2011, 485 - 496, Smith SMDownload Item:
Abstract:
Although membrane proteins account for 20–30% of the coding regions of all sequenced genomes and
play crucial roles in many fundamental cell processes, there are relatively few membranes with known 3D
structure. This is likely due to technical challenges associated with membrane protein extraction, solubili
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sation, and purification. Membrane proteins are classified based on the level of interaction with membrane
lipid bilayers, with peripheral membrane proteins associating non-covalently with the membrane, and
integral membrane proteins associating more strongly by means of hydrophobic interactions. Generally
speaking, peripheral membrane proteins can be purified by milder techniques than integral membrane
proteins, whose extraction requires phospholipid bilayer disruption by detergents. Here, important criteria
for strategies of membrane protein purification are addressed, with a focus on the initial stages of membrane
protein solublilisation, where problems are most frequently encountered. Protocols are outlined for the
successful extraction of peripheral membrane proteins, solubilisation of integral membrane proteins, and
detergent removal which is important not only for retaining native protein stability and biological func
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tions, but also for the efficiency of later purification techniques
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Author: SMITH, SINEAD
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Methods in Molecular BiologyPublisher:
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