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Protein Folding Notes

Pharmacology Notes > BIOL10212 Biochemistry Notes

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Biochemistry - Lecture 13 (12/03/2018)

Protein Folding

Polypeptide chains are synthesized as linear polymers of amino acids,
and are joined by peptide bonds.
The process by which the polypeptide chains adopt their functional 3D
shape is through Protein Folding.

Why a defined 3D shape is necessary

For most proteins, their biological function requires them to adopt a defined 3D shape.

For example, catalysis requires a very high degree of atomic alignment.
In addition, protein-substrate, protein-protein interactions require a high level of shape complementarity for molecular recognition.

Hence the final folded structure needs to be accurate and often within the width of one atom.

Misfolding is wasteful and in some cases, it can be dangerous and cause disease.

Mutations can cause misfolding and result in disease, as it can cause the loss of function of a critical enzyme or receptor, resulting in the formation of toxic aggregates and an abnormal cell morphology, which can, for example, cause abnormal collagen assembly or deficient connective tissue.

This can include:

Mislocalisation - Where the protein is not transported to its final destination, this can cause accumulation in the ER, degradation, loss of functional enzymes, receptors and tumour suppressors.

Extracellular toxic aggregates - This can cause amyloid plaques, intracellular deposits and is neurodegenerative.

Abnormal collagen or extracellular matrix protein assembly - This involves connective tissue diseases.

Abnormal cell or tissue morphology - This can cause impaired function.

Extracellular Toxic Aggregates
Abnormal Collagen or Extracellular
Matrix Protein Assembly

Exceptions to the rule

Abnormal Cell or Tissue

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