Daniel K. Clare

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The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP binding initiates a series of conformational changes triggering the association of the cochaperonin GroES, followed by further large movements that eject the substrate polypeptide from hydrophobic binding sites into a(More)
Low dose electron imaging applications such as electron cryo-microscopy are now benefitting from the improved performance and flexibility of recently introduced electron imaging detectors in which electrons are directly incident on backthinned CMOS sensors. There are currently three commercially available detectors of this type: the Direct Electron DE-20,(More)
Micro-ID is a new test system designed to identify members of the family Enterobacteriaceae in 4 h. It consists of 15 biochemical tests on reagent-impregnated paper disks; each test is in its own compartment in a molded plastic tray. Based on the pattern of positive and negative biochemical reactions, a five-digit octal code number is calculated. A(More)
A 21-residue peptide analog of the Ca2+ binding Site 3 in rabbit skeletal troponin C has been synthesized by the solid phase method. CD studies as well as uv difference spectroscopy did not show any changes upon addition of Ca2+ to this peptide in aqueous solution. Acetylation of the NH2-terminal residue of the analog resulted in Ca2+-induced CD and uv(More)
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