Abstract
The structures of the interfaces of nine dimeric and nine tetrameric proteins have been analyzed and have been seen to follow general principles. These interfaces are combinations of four structural motifs, which resemble features of monomeric proteins. These are: (i) extended beta sheet; (ii) helix-helix packing; (iii) sheet-sheet packing; and (iv) loop interactions. Other common structural features in the interfaces studied are two-fold symmetry, charged hydrogen bonds and channel formation (found only in tetramers). Monomer-monomer interfaces are intermediate in hydrophobicity and charge between the interfaces between secondary structures of monomeric proteins and the exteriors of monomeric proteins. A typical interface has one of the first three of the structural motifs at its centre and loop interactions around the outside, where most of the charge resides.
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