Brandon C. and Tooze J. 1999. /niröf/uefion fo protein structure, 2nd edition. Garland Publishing, New York.

Pauling L. 19GU. The nature of the chemical hond, 3rd edition. Cornell University Press, tlhaea. New York,

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

Chothia C. 1984. Principles that determine the structures of proteins. Ann. Rev. Biochem. 53: 537-572.

Most Proteins Are Modular, Containing Two or

Three Domains

Rose G.E, 1979. HiereraTchical organization of domains in globular proteins. /. Mol. Biol. 134: 447-470.

Steitz T.A., Weber !.*!., and Matthew j.B 1982, Catabotite gene activator protein: Structure, homology, with other proteins, and cyclic AMP and DNA binding. CtiM Spring Harbor Syrnp. in Quant. Bio. 47: 419-426.

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

De Cuzman R.N., tamer R.B., and Summers M.F. 1999. Prntein-RNA recognition. Biopolymers 48: 181-195.

Sperling R. and Wachtel EJ. 1981. The histones. Adv. Prot. Chem. 34: 1-52.

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

Reil C.E and Lewis M. 21)01. The l^ac repressor: A second generation of structural and functional studies. Cur. Opin. in Struct. Bio. 11:19-25.

Pace H.C., Kercher M.A., Lu P., Markiewicz P., Miller J.H., Chang G., and Lewis M. 1997. Lac repressor genetic map in real space. TIBS 22: 334-338.

Pavletich N.F. 1999, Mechanisms of cyclin-dependent kinase regulation; Structures of cdks, their cyclin activators, and cip and INK4 inhibitors, /. Mol Bin}, 287; 821-828.

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