Mapping of hydrophobic sites on the surface of myosin and its fragments

Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling

“…Niwa et al (1986) reported that changes in the hydrophobicity of actomyosin after freezing are due to myosin rather than to actin. Native myosin has hydrophobic residues strongly concentrated in the core of the helix (Maclachlan & Karn, 1982) and the surface of the helix is essentially devoid of hydrophobic groups (Borejdo, 1983). In this way, the lower surface hydrophobicity of AME1 could be due to a greater stability of this protein than that of AME2, suggesting some influence of the catch method on the protein stability.…”

Biochemical and physicochemical properties of actomyosin from pre- and post-spawned flounder (Paralichtys patagonicus) stored on ice

“…Native myosin has hydrophobic residues strongly concentrated in the core of the helix (MacLachlan & Karn, 1982). The surface of the myosin helix has a high density of charged groups and is essentially devoid of hydrophobic groups (Borejdo, 1983). Therefore, conformational changes in actomyosin could be monitored following the unfolding of the a-helical portion of myosin with exposition of the previously hidden hydrophobic core.…”

Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs

“…Niwa et al (1986) reported that changes in the hydrophobicity of actomyosin after freezing are due to myosin rather than due to actin. Native myosin has hydrophobic residues strongly concentrated in the core of the helix (McLachlan & Karn, 1982) and the surface of the helix is essentially devoid of hydrophobic groups (Borejdo, 1983). In this way, the lower superficial hydrophobicity of Aulacomya actomyosin could be due to a greater stability of this protein before the chemical environment.…”