Over on the website of the UK Centre for Intelligent Design, Anthony Latham (author of The Naked Emperor: Darwinism Exposed) has an excellent article on a recent review article in Nature on the role of molecular chaperones in protein folding. Latham writes,
The journal Nature has just published a detailed and fascinating review about the way proteins in our bodies are helped by other proteins, known as chaperones, to become functional.
Proteins are the most complex molecules in our bodies and are involved in virtually all biological processes. Our cells typically manufacture over 10,000 different proteins, synthesised on ribosomes as chains of up to several thousand amino acids.
For a protein to function it must fold to its ‘native state’ which is a complex three-dimensional structure. If a protein fails to fold into its functional structure then it is not only without function but in many cases is actually toxic to the cell. It is thought that as we age, the systems for helping proper folding work less well, which is one of the reasons for the symptoms of ageing and some diseases.
The number of possible shapes that a protein can fold into is very high and folding reactions are very complex, involving the co-operation of many weak, non-covalent interactions. A high percentage of proteins do not fold automatically into the required shape and are at risk of aberrant folding and aggregation. As the abstract to this paper states: “To avoid these dangers, cells invest in a complex network of molecular chaperones, which are ingenious mechanisms to prevent aggregation and promote efficient folding.”