Molecular dynamics analyses were performed to examine conformational changes in the C-domain of calmodulin and the N-domain of troponin C induced by binding of Ca(2+) ions. Analyses of conformational changes in calmodulin and troponin C indicated that the shortening of the distance between Ca(2+) ions and Ca(2+) binding sites of helices caused widening of the distance between Ca(2+) binding sites of helices on opposite sides, while the hydrophobic side chains in the center of helices hardly moved due to their steric hindrance. This conformational change acts as the clothespin mechanism.
View Article and Find Full Text PDFA 23-year-old man was admitted to our hospital because of cough and sputum in April 2001. A chest roentgenogram revealed infiltrative shadow with cavity formation in the bilateral lung fields. He was treated with sensitive antituberculous drugs.
View Article and Find Full Text PDFA 20-year-old woman was admitted to our hospital because of cough and dyspnea in April 2001. On admission, laboratory data showed positive inflammatory signs. A chest roentogenogram revealed infiltrated shadow in the bilateral lung fields.
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