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Electrostatic Mechanism
Peripheral membrane proteins interact with lipids through electrostatic mechanisms. In lipid-protein membrane behavior, proteins prefer solid phase interactions due to precise hydrophobic matching. Proteins prefer hydrophobic matching since this phase is a driving force of stability and binding precision. In the cases where peripheral protein association with the membrane is achieved by interaction with lipid headgroups, the nature of this association is mostly reversible. Experiments using mass spectrometry (MS) has shown that negatively charged lipids bind differential to the outer membrane porin were found to affect opening and closing times.