Thermal decomposition and microemulsion are generally stabilized in an organic solvent by surfactants.
Polar surfaces are generally stabilized by surface reconstruction or faceting; transfer of charge between surfaces or surface nonstoichiometry, including the neutralization of surface charge by adsorbed molecules.
This metabolite is generally stabilized through conjugation with glutathione by glutathione s-transferase (GST) (Henderson et al. 2000) and eliminated via the kidney.
Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a hydrophobic core, but also through salt bridges, hydrogen bonds, disulfide bonds, and even posttranslational modifications.
In addition, anticancer peptides are generally stabilized by the disulfide bonds.
This property explains that the complex formation between fusion proteins is generally stabilized by the association of split fragments, allowing the visualization of weak and transient interactions.
U-turn structures are generally stabilized by two hydrogen bonds involving the required U residue: U 2′ OH to R N7 and U H3 to R 3′-phosphate.
Moreover, IAA28myc protein was less abundant in ibr5, which is not expected if Aux/IAA proteins are generally stabilized, also suggesting that IBR5 modulates auxin-responsive transcription without stabilizing Aux/IAA proteins.
Fourth, and most importantly, unlike known RNA protein interactions, which are generally stabilized by electrostatic forces, as described earlier, the aptamer bound to the neutral portion of the hFc1 surface (Fig. 1D) and the aptamer hFc1 interaction was stabilized by multiple weak interactions such as hydrogen bonds and van der Waals forces (Nomura et al. 2010).
It discusses model proteins systems into which highly fluorinated amino acids have been introduced and the reasons why fluorinated residues are generally stabilizing, with particular reference to thermodynamic and structural studies from our laboratory.
