Abstract
Optimal application of protein engineering technology will require understanding how the amino acid sequence of a polypeptide chain specifies its spatial conformation. It is now clear that polypeptide chain folding and subunit assembly proceeds through sequential pathways involving defined intermediates. The critical amino acid instructions directing these pathways appear to be dispersed through the sequence. Recent genetic approaches have begun to identify which residues in a chain are important in maintaining the pathway, and avoiding aggregated states. Investigations of the P22 tailspike endorhamnosidase suggest that one general class of mutants, tss mutants, may be particularly informative in identifying sequences determining the conformation of the intermediates. Certain inherited human diseases may represent single amino acid substitutions causing folding defects.
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