Tertiary Protein Structure

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This is where the protein folds in on itself and forms a complex three dimensional structure. This is structure is held together by many different types of interactions between the 'R' groups on the amino acids. The various types of interactions are as follows ionic interactions, hydrogen bonds, van der Waals forces or disulphide bridges [1] but which of these occur does depend upon on what amino acids are present in the sequence and which others they are close to interact with.

A Diagram of a proteins tertiary structure is shown to the right [2].
Hemoglobin ribbon 4subunits.jpg
This is an image of a Heamoglobin molecule and you can see from the image that there are mulitple protein sequences interacting with themselves and each other.

The tertiary structure of a protein is highly important as it is the 3D shape of the protein that affects its function. If altered it can have severe implications for the carrier of this mutation as it would affect the proteins ability to recognise and bind to its substrate and bind if it were an enzyme, recognise and transmit signal if it was a receptor or if recognised in read through be destroyed before even reaching the membrane [3]. Mutations will usually result in a disease as proteins are present in almost all vital bodily functions. Examples of protein mutation causing disease are Cystic fibrosis, Sickle Cell anaemia.

Heat can often change the tertiary structure of enzymes, as it can break the bonds holding the structure together.

References

  1. http://www.chemguide.co.uk/organicprops/aminoacids/proteinstruct.html
  2. ttp://www.bio.davidson.edu/Courses/Molbio/MolStudents/spring2005/Heiner/hemoglobin.html
  3. http://genome.wellcome.ac.uk/doc_WTD020766.html

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