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Non-Covalent Interactions In Proteins

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Which non covalent interactions are most likely to be important in protein-protein interactions in aqueous environment?

What is the driving force for proteins that are embedded in lipid membranes?

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Solution Summary

The solution comprises of a detailed 540 word explanation of important protein-protein interactions in an aqueous environment, and the driving force for proteins that are embedded in lipid membranes.

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As you know, there are four main types of non-covalent interactions: ionic bonds (or electrostatic interactions), van der Waals forces, hydrogen bonds, and hydrophobic interactions.

Ionic bonds occur between charged groups and can be very strong individually. However, if there are too many of them, they can operate as repulsion forces between proteins because "like charges" (negative/negative or positive/positive) will repel each other. Therefore, although they can stabilize a protein-protein interface, they do not drive its formation. They act more as forces that govern the specificity of the interaction. Generally, if you increase the electrostatic charges on proteins, you dissociate them!

van der Waals forces are dipole-dipole interactions that are weak individually, but can sum up to quite a large force collectively. Once again, they do not drive the ...

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