Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation.
CA Haase-Pettingell, J King - Journal of Biological Chemistry, 1988 - ASBMB
The in vivo accumulation of polypeptide chains in the form of aggregated non-native states
is a problem in many applications of biotechnology. In the maturation pathway of the
thermostable P22 tailspike endorhamnosidase, the folding and chain association
intermediates can be distinguished from the native tailspikes in crude extracts of phage-
infected Salmonella cells. Temperature-sensitive folding mutations, at many sites in the
chain, destabilize these conformational intermediates preventing the formation of native …
is a problem in many applications of biotechnology. In the maturation pathway of the
thermostable P22 tailspike endorhamnosidase, the folding and chain association
intermediates can be distinguished from the native tailspikes in crude extracts of phage-
infected Salmonella cells. Temperature-sensitive folding mutations, at many sites in the
chain, destabilize these conformational intermediates preventing the formation of native …
