Quaternary Structure

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Proteins have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of polypeptide chains interact with each other by forming a range of bonds such as Hydrogen bond, disulphide bridges/bonds and many more. Each polypeptide chain can vary in their genes they were coded from. An example of a quaternary structure protein is haemoglobin.
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[[Proteins|Proteins]] have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of&nbsp;[[Polypeptide|polypeptide chains]]&nbsp;interact with each other by forming a range of bonds such as [[Hydrogen bond|hydrogen bond]], [[Disulphide bridges|disulphide bridges/bonds]] and many more. Each polypeptide chain can vary in their genes they were coded from. An example of a quaternary structure protein is [[Haemoglobin|haemoglobin]]<ref>Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.</ref><ref>Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.</ref><br>
  
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=== References  ===
  
 
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<references />
<ref>Millar, T (2006). Biochemistry explained. New York: Taylor &amp; Francis. 51.</ref>
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Latest revision as of 01:45, 24 October 2014

Proteins have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of polypeptide chains interact with each other by forming a range of bonds such as hydrogen bond, disulphide bridges/bonds and many more. Each polypeptide chain can vary in their genes they were coded from. An example of a quaternary structure protein is haemoglobin[1][2]

References

  1. Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.
  2. Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.
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