Counteracting Effect of Charged Amino Acids Against the Destabilization of Proteins by Arginine

Chain Compaction and Synergistic Destabilization of Globular Proteins by Mixture of Denaturants

“…Further, the addition of Arg to the native proteins marginally decreases the V ° values even in the absence of Gdm. An earlier study revealed that the addition of 1 M of Arg does not alter the globular structure of both the proteins significantly . Therefore, this marginal decrease could arise from the interaction of surface residues with Arg which reduces the water solvation around the proteins.…”

“…Also, the increase in Arg concentration decreases the K s values consistently even in the presence of Gdm. As mentioned earlier, Arg alone does not significantly unfold the proteins even at the concertation of 1 M, therefore, this reduction in K s values might arise due to the direct interaction of the osmolyte with the surface residues which might weaken the surface hydration of the proteins. It may be noted that V o and K s values do not show any additive effects in the mixture of Gdm and Arg as their combined effect on protein surface hydration may be different from their individual effects.…”

“…An earlier study revealed that the addition of 1 M of Arg does not alter the globular structure of both the proteins significantly. [17] Therefore, this marginal decrease could arise from the interaction of surface residues with Arg which reduces the water solvation around the proteins. In addition to this, the V°F igure 2.…”

Partial incubation-induced changes in concentrations of egg white antimicrobials do not influence trans-shell infection but affect hatchling phenotype

“…In any case, previous studies documented that lysozyme decrease in egg white owing to incubation is a result of proteins aggregation 42,43 , binding of lysozyme to other proteins 73 , or lysozyme degradation early after incubation . Yet, most recent works revealed that thermal aggregation of proteins and resulted changes in protein abundances were highly dependent on the content of particular amino acids such as arginine, lysine or aspartic acid acting as protein stabilizer and/or destabilizers 74,75 . Moreover, temperature-induced level of proteins aggregation was found to be linked with the concentrations of other heat-sensitive egg white proteins such as ovotransferrin 76 .…”

Peer Review #1 of "Temperature-induced changes in egg white antimicrobial concentrations during pre-incubation do not influence bacterial trans-shell penetration but do affect hatchling phenotype in Mallards (v0.1)"

“…While this might suggest that different embryonic developmental stages are playing a role (see Guyot et al 2016b), other studies have suggested that egg-white lysozyme decreases due to protein aggregation (Liu et al 2015;Qiu et al 2012), lysozyme binding to other proteins (Kato et al 1975) or lysozyme degradation soon after incubation (Fang et al 2012a). Recent works, however, have suggested that thermal aggregation of proteins, and the resulting changes in protein abundance, are highly dependent on the content of particular amino acids, such as arginine, lysine or aspartic acid, which act as protein stabilisers and/or destabilisers (Anumalla & Prabhu 2019;Hong et al 2017). Further, temperature-induced levels of protein aggregation have been shown to be linked with the concentration of other heat-sensitive egg-white proteins, such as ovotransferrin (Iwashita et al 2019).…”