02 Protein Folding

02 Protein Folding - Protein Folding Although any protein...

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Protein Folding Although any protein primary structure could fold in many different ways any given protein always folds in the same way, to form the most stably folded form of the molecule. This is called the native state . It has been shown experimentally that many proteins, when unfolded by high concentrations of urea, will refold into the native state when the urea is removed by dialysis. This is evidence that the native state can form automatically, as a consequence of the primary structure of the protein, without input from any enzymes or co-factors. However, parts of the folding process are relatively slow, and in the high concentration of proteins in the cell errors are likely to occur if folding cannot occur at a faster rate than the spontaneous in vitro process. In addition folding can start to occur as the protein emerges from the ribosome during synthesis, and this may result in an abnormal folding. It may be necessary to hold the protein in an extended form until synthesis is complete if a native state folding is to occur.
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Enzymes Involved in Folding There are two important processes in protein folding which are slow if they happen spontaneously, but are speeded up enzymicaly in the cell. The peptide bond linking proline residues into the primary structure has cis – trans isomers. In forming the protein fold it is important that these are in the correct form. Spontaneous isomerisation is slow, and switching an
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This note was uploaded on 02/25/2012 for the course CHEM 1341 taught by Professor Compton during the Fall '08 term at Texas State.

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02 Protein Folding - Protein Folding Although any protein...

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