The Importance of Normal and Aberrant Protein Folding in Biology

2 The Importance of Normal and Aberrant Protein Folding in Biology 

Natural proteins are able to fold to specific structures because, on average, native-like interactions between residues are more stable than non-native ones. The former are therefore more persistent and the polypeptide chain is able to find its lowest energy structure by a process of trial and error. Moreover, if the free energy surface or landscape has the right shape (see Fig. 13.1), only a minute fraction of all possible conformations is sampled by any given 

Alzheimer s disease0 Amyloid P peptide 40 or 42d Natively unfolded 

Huntington s diseasef Huntingtin with 3,144s Largely natively 

AL amyloidosis0 Immunoglobulin light chains or fragments thereof ca. 90d All-P, IG-like 

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