Protein distribution in egg whites is as follows: (54%) ovalbumin, (13%) conalbumin/ ovotransferrin, (11%) ovomucoid, (4%) ovoglobulins, (3.5%) lysozyme, and (2%) ovomucin.
Ovoglobulins drive foaming, ovomucin is the main stabilization agent, and the remainder of the proteins interact to contribute to overall foaming and stability.
When egg whites are beaten, some of the hydrogen bonds in the proteins break, causing the proteins to unfold ("denature") and to aggregate non-specifically.
When these egg white proteins denature (due to agitation from beating), their hydrophobic regions are exposed and the formation of intermolecular protein-protein interactions is promoted.
These protein-protein interactions, usually disulfide bridges, create networks responsible for the structure of the foam and this change in structure leads to the stiff consistency required for meringues.
The use of a copper bowl, or the addition of cream of tartar is required to additionally denature the proteins to create the firm peaks, otherwise the whites will not be firm.
Wiping the bowl with a wedge of lemon to remove any traces of grease can often help the process.

When beating egg whites, they are classified in three stages according to the peaks they form when the beater is lifted: soft, firm, and stiff peaks.

Egg whites and sugar are both hygroscopic (water-attracting) chemicals.
Consequently, meringue becomes soggy when refrigerated or stored in a high-humidity environment.
This quality also explains the problem called "weeping" or "sweating", in which beads of moisture form on all surfaces of the meringue.
Sweating is a particular problem for French meringues in which the granulated sugar is inadequately dissolved in the egg whites, and for high-moisture pie fillings.
Protein distribution in egg whites is as follows: (54%) ovalbumin, (13%) conalbumin/ ovotransferrin, (11%) ovomucoid, (4%) ovoglobulins, (3.5%) lysozyme, and (2%) ovomucin. Ovoglobulins drive foaming, ovomucin is the main stabilization agent, and the remainder of the proteins interact to contribute to overall foaming and stability. When egg whites are beaten, some of the hydrogen bonds in the proteins break, causing the proteins to unfold ("denature") and to aggregate non-specifically. When these egg white proteins denature (due to agitation from beating), their hydrophobic regions are exposed and the formation of intermolecular protein-protein interactions is promoted. These protein-protein interactions, usually disulfide bridges, create networks responsible for the structure of the foam and this change in structure leads to the stiff consistency required for meringues. The use of a copper bowl, or the addition of cream of tartar is required to additionally denature the proteins to create the firm peaks, otherwise the whites will not be firm. Wiping the bowl with a wedge of lemon to remove any traces of grease can often help the process.
When beating egg whites, they are classified in three stages according to the peaks they form when the beater is lifted: soft, firm, and stiff peaks.
Egg whites and sugar are both hygroscopic (water-attracting) chemicals. Consequently, meringue becomes soggy when refrigerated or stored in a high-humidity environment. This quality also explains the problem called "weeping" or "sweating", in which beads of moisture form on all surfaces of the meringue. Sweating is a particular problem for French meringues in which the granulated sugar is inadequately dissolved in the egg whites, and for high-moisture pie fillings.
Meringue