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The Specific Conformation of a Protein Results from Its Pattern of Hydrogen Bonds

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Most Proteins Are Modular, Containing Two or

Three Domains

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lions, often regulate protein function through «Hosiery. That is, the ligand binds (or the modification targets) a site on the protein separate from the region of that protein that mediates its main function (the active site of an enzyme, DNA-binding domain, etc). This binding or modification triggers a change in the shape of the protein which increases or decreases the activity of the active site, or DNA-binding domain, essentially switching the activity on or off.

In uther cases, a protein may be controlled by modification or binding of a second protein, in ways that do not involve alioKtery. For example, modification can create a site on a protein that is recognized by a second protein. Such protein-protein interactions can recruit proteins to particular locations or substrates, and in that way control their activity.

Weak Bonds Correctly Position Proteins along DNA and RNA Molecules

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Allostery: Regulation of a Protein's Function by Changing Its Shape

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