Abstract
ABSTRACTThe relationship between solubility and conformational changes of salmon (Oncorhynchus tshawytscha) myofibrillar proteins at various ionic strengths and pH was investigated using myosin as a model system. Solubility of myosin increased with increased KCl concentration up to 0.5M. Further increasing salt concentration resulted in a gradually reduced solubility. In the absence of salt, myosin was slightly soluble at pH>7 or <4. The increased solubility correlated with the increased surface hydrophobicity and relative sulfhydryl content as well as the decreased α‐helicity. At KCl >1.0M, myosin regained its helix structure with a concomitant loss of solubility due to the dominant hydrophobic interaction among nonpolar amino acid residues.
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