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Mechanisms involved in the formation of three‐dimensional networks of globular proteins are discussed in general terms. Denaturation and aggregation of soy proteins under various conditions were studied. Differential scanning calorimetry was used in the denaturation, and turbidity measurements in the aggregation studies. Conditions favoring denaturation, such as high and low pH, had the opposite effect on aggregation. Salt was found to have a special effect on the behavior of soy proteins, suppressing aggregation as well as denaturation, probably due to its stabilizing influence on the quaternary structure. Viscometric studies of the progel state of soy protein gels showed that the onset of the progel is closely related to the denaturation process. Some commercial isolates were found to be completely denatured. Despite forming firm gels after cooling, they did not appear to have a progel state.

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