BCH2011 Lecture Notes - Lecture 7: Peptide, Ferrous, Hydrophile

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Many proteins gave multiple polypeptide subunits (from two to hundreds). Many multisubunit proteins have regulatory roles; the binding of small molecules may affect the interaction between subunits, causing large changes in the protein"s activity in response to small changes in the concentration of substrate or regulatory molecules. A multisubunit protein is also referred to as a multimer. A multimer with just a few subunits is often called an oligomer. If a multimer has nonidentical subunits, the overall structure of the protein can be asymmetric and quite complicated. However, most multimers have identical subunits or repeating groups of nonidentical subunits usually in symmetric arrangements. The repeating structural unit in such a multimeric protein, whether a single subunit or a group of subunits, is called a protomer. The first oligometric protein to have its 3d structure determined was haemoglobin, which contains four polypeptide chains and four heme prosthetic groups, in which the iron atoms are in the ferrous (fe2+) state.

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