Sentence examples for native packing from inspiring English sources

Thermal denaturation of RIα leads to partial loss of native packing with exposure of aggregation-prone motifs, such as the B' helices in the phosphate-binding cassettes of both CNB domains.

In conclusion, our results indicate that thermal denaturation of RIα involves a partial loss of native packing (native state → partially unfolded), as suggested by DSC and MD simulations, with subsequent self-association via β-type aggregation (partially unfolded → cross-β-intermolecular aggregates → disc-like soluble aggregates), as indicated by CD, ThT fluorescence and AFM experiments.

The MD simulations of TRPZ1 provide evidence that the rate-determining steps for the unfolding consist in the disruption of the native packing of the hydrophobic core (i.e., transition from N to I).

The formation of non-native interactions during folding is not exclusive to all-α-helical proteins: non-native packing of hydrophobic sidechains has also been shown to play an important role in stabilizing the intermediates formed during the folding of α-lactalbumin [ 60], lysozyme [ 61], SH3 domains [ 35 ] and CD2.d1 [ 55].

Mutational analysis of apomyoglobin has shown that truncation of residues in helices G and H that make no contact in the native state results in destabilization of its burst phase intermediate, consistent with this species adopting a native-like fold stabilized by non-native packing contacts between these helices [ 56].

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Thus, the data presented here point to the disruption of the native hydrophobic packing as the main rate-limiting step of the unfolding reaction.

A further difference from GB1 is that the slowest process in TRPZ1 unfolding is the disruption of the native hydrophobic packing (N→I transition) while in GB1 the F→H transition is considered to be rate-determining (45).

In addition, the CD spectrum of the aggregated Trpzip2-K sample shows clearly the presence of a positive band at 228 nm, indicating that the native Trp Trp packing is preserved to a certain extent in the aggregates.

Analysis of the un/folding kinetics and classical commitment probability calculations on the conformations extracted from the transition pathways show that the rate-limiting step for unfolding is the disruption of the ordered native hydrophobic packing (Trp-zip motif) leading from the native to the intermediate state.

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