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Globular domains of proteins tend to be generated at high frequency by independent duplications or selective pressure. These domains are small (from 6 to 25 amino acids) and often extend the amino or carboxy terminus of the primary structure, thus affecting the secondary and tertiary structure of the polypeptide chain. They often have a folded conformation and are involved in binding calcium. They usually form as a pair of antiparallel helices with the calcium ion located at the tip of one of the helices. In the case of calmodulin, it is possible to predict the functional domains of the molecule based on the conformation of the three domains it contains. In addition, three polyvalent binding sites have been identified in calmodulin. Two are formed by the binding of two calcium ions and the third is at the interface of the two domains in which the calcium ions reside. In order for binding of the domains of calmodulin to the two calcium ions to be possible, these must adopt a conformation complementary to the position they hold in the folding structure. Consequently, it can be predicted that an as yet unidentified calcium-binding protein will be multidomain. The two most likely types of additional domains are found in globular proteins and are either tightly packed loops of the chain or extended calmodulin-like helices. Both types have been identified as calcium-binding proteins. Of the five putative calcium-binding proteins (haem-binding protein, calmodulin, troponin C, ATPase, and two-headed calmodulin) identified in the Murein hydrolase-digesting Spiroplasma erythraea, only two appear to possess calmodulin-like domains.[Quality improvement in mental care during a course of nursing: effects on quality of life and subjective social support].
Mental health care is known to be associated with negative effects on quality of life (QOL) and subjective social

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