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Because protein structures are the result of their amino acid sequences, some changes can dramatically change the properties of a protein by destabilizing the structure or changing the surface of the protein in a way that changes its interaction with other proteins and molecules.
Contacts involving many beta-branched hydrophobic residues in the crowded protein core may generate strain in helices, destabilizing the structure.
Low levels of proBias enabled fissures to reach toward the SMS center, destabilizing the structure and causing chaotic, uncontrolled growth.
Furthermore, all nonsense or mutations of deletion in Gigaxonin are likely severely destabilizing the structure, by improper folding of the β-propeller that constitutes the KELCH domain.
Overall, our results are consistent with previous reports that correlate these FRS mutations to disease states by affecting aminoacylation activity as well as destabilizing the structure of FRS [ 58].
Similar(55)
Thus, the introduction of a negative charge at position 18 destabilizes the structure of Hha.
We speculate that mutation of a self-contacting residue in the buried or partially buried region of a protein will destabilize the structure.
From UV melting studies we showed a position dependent effect of UNA modifications such that quadruplexes with UNA modified loops are further stabilized whereas UNA modifications in stem of the G-quadruplex significantly destabilize the structure.
The presence of both, negatively charged gold nanoparticles (NPs) and gold cations was crucial for the activation of 2,4-dichlorobenzaldehyde via the interaction with chlorine substituent atoms and aldehyde oxygen atoms as well as breaking of the "pseudo hydrogen bond" between aldehyde hydrogen atom and chlorine substituent, which destabilized the structure making it more active.
The changes at these two positions destabilized the structure of the protein.
Furthermore, substitutions of K14, by affecting early kinetics and assembly, could destabilize the structure of the final assembly or drive the assembly into a different pathway, which would lead to different morphologies for the aggregates.
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