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Investigating the Effect of Sidechain Packing on Membrane Protein Association

Gilbert Jamilla Loiseau

出版	ProQuest LLC, 2024
URL	http://books.google.com.hk/books?id=ih8O0QEACAAJ&hl=&source=gbs_api

註釋

Membrane protein folding occurs as a result of an equilibrium of biophysical forces. Polar and charged interactions can drive folding within the hydrophobic environment of the membrane. The stabilizing effects of sidechain packing on membrane protein folding were deduced in a variety of foundational bacteriorhodopsin studies, and sidechain packing as a driving force has been demonstrated through modern protein re-design of phospholamban. However, the extent at which packing can act as a driving force in general in membrane protein systems is not well understood. We investigate the impact of sidechain packing on membrane protein association by using computational design. By sampling dimer conformations from the PDB, we designed hundreds of sequences that self-associate. Structural characterization through mutations on these proteins suggests that packing is a weak driving force in a variety of membrane protein systems.