Quaternary structures: Difference between revisions
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A quaternary structure is a protein structure composed of two or more [[Polypeptide]] chains. The quaternary structure is held together by a combination of [[Hydrogen bonds]], disulphide bridges and [[Ionic bonds]]<ref>http://www.particlesciences.com/news/technical-briefs/2009/protein-structure.html</ref>. They often also contain an inorganic group called a [[Prosthetic group|prosthetic group]]. An example of a quarternary protein that contains the prosthetic Haem group is [[Haemoglobin]]<ref>https://alevelnotes.com/Protein-Structure/61</ref>. Haemoglobin is composed of two Alpha polypeptide chains and two Beta polypeptide chains, the Haem group contains four Fe<sup>2+</sup> ions which oxygen binds to in order for the protein to transport oxygen around the body. As it contains four Fe<sup>2+</sup> ions, when it has four [[Oxygen]] molecules bound it is known as being saturated and is carrying<ref>http://www.thealevelbiologist.co.uk/haemoglobin</ref>. | |||
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Latest revision as of 19:28, 30 November 2017
A quaternary structure is a protein structure composed of two or more Polypeptide chains. The quaternary structure is held together by a combination of Hydrogen bonds, disulphide bridges and Ionic bonds[1]. They often also contain an inorganic group called a prosthetic group. An example of a quarternary protein that contains the prosthetic Haem group is Haemoglobin[2]. Haemoglobin is composed of two Alpha polypeptide chains and two Beta polypeptide chains, the Haem group contains four Fe2+ ions which oxygen binds to in order for the protein to transport oxygen around the body. As it contains four Fe2+ ions, when it has four Oxygen molecules bound it is known as being saturated and is carrying[3].