AbstractMyosin was isolated from bovinem. semimembranosusand gels were formed by heat treatment at different pH values and ionic strengths. The gels were subjected to rigidity measurements and their microstructure was studied by scanning electron microscopy. This article provides evidence that myosin can form two completely different gel structures in the pH range 5.5–6.0, depending on ionic strength. Fine stranded gel structures were formed at low ionic strength (0.25M KCl), whereas coarsely aggregated gel structures were formed at high ionic strength (0.6M KCl). The fine stranded structure had a higher rigidity than the coarsely aggregated structure. It was found that all fine strand myosin gels were formed from turbid solutions and the aggregate gels from clear solutions. When the pH was lowered to 4 in 0.6M KCl a strand‐type gel structure formed spontaneously on dialysis, even without heat treatment. This structure did not change in character on heating. It was concluded that the conditions required for the formation of strand‐type myosin gels were already present before the heat treatment and that the strands were made up of myosin filaments at certain pH and ionic strength combinations, which produced a turbid solution. The strand‐type structures were considered specific with regard to myosin interactions which was not the case for the aggregated structures. Variation of the heating temperature in the range 55 to 65°C had no major effect on the type of structur