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The chemical properties of cytosine present cells with a serious informational ‘disease’, necessitating enzymes with exquisite specificity for deoxyuridine for its prevention and cure.
New evidence for partial specific tertiary interactions within an apomyoglobin folding intermediate force reexamination of the role of specific contacts in stabilizing the molten globule.
Studies on various thermostable hydrophobic core mutations of α1-antitrypsin reveal a single consensus mechanism maintaining the native strain within this metastable protein.
Unanticipated similarities between apo-calmodulin and the myosin essential light chain suggest structural characteristics responsible lor IQ-motif binding as well as calcium induced conformational changes.