CCT undergoes multiple rounds of ATP-dependent interaction with unfolded α-tubulin polypeptides, forming chaperonin bound quasi-native tubulin folding intermediates that contain a GTP binding pocket (Tian et al., 1995).
Interaction of unfolded OMPs with Skp is thought to occur early after translocation across the IM, as evidenced by the ability to cross-link Skp to the OMP PhoE at the periplasmic side of the IM in spheroplasts [101].
Local hydrophobic collapse of the polypeptide chain and transient long-range interactions in unfolded states of apomyoglobin appear to occur in regions of the amino acid sequence which, upon folding, bury an above-average area of hydrophobic surface.
Both the defined oligomers and the generalized intra-lane background (the latter likely reflecting BiP interactions with unfolded client proteins) were diminished and replaced by a prominent high mobility species (labeled 'B' form, Figure 8A, lanes 1 and 2).
This intermediate is characterized by premature interaction of the unfolded domains, and particularly involving unfolded VH, independent of proline cis trans isomerization in VL.
This parameter is a scale of the hydrophilic interaction of the unfolded state.
The increased hydrophobicity of these recombinants may be important for their better interaction with partially unfolded target proteins as compared to PDC-109 andne and prevention of their aggregation.
The lipid/protein recombinants possess a higher surface hydrophobicity as compared to native PDC-109, which could be responsible for their better interaction with partially unfolded proteins and prevention of their aggregation under stress conditions.
Apart from the proteasome route, misfolded proteins (polymerized through hydrophobic interaction of partially unfolded polypeptides and leading to the formation of cytoplasmic scattered structures, inclusion bodies and aggregosomes) can be targeted to degradation by macroautophagy (Kopito, 2000).
As such, assembly into either fibrils or sheets likely represents intermolecular interactions occurring from unsatisfied protein protein or protein ligand interactions in the unfolded ensemble.
Of interest is that ionisable group interactions in the unfolded state appear to be dominated by local sequence neighbours, in part recapitulating the interactions of the folded state [ 29].
