Kathleen E. Orrell
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View article: Structure-function analysis of distant diphtheria toxin homologs reveals insights into host adaptation
Structure-function analysis of distant diphtheria toxin homologs reveals insights into host adaptation Open
Diphtheria toxin (DT) is the archetype of bacterial exotoxins implicated in human diseases and has played a central role in defining the field of toxinology since its discovery in 1888. Despite being one of the most extensively characteriz…
View article: Intestinal bile acids directly modulate the structure and function of <i>C. difficile</i> TcdB toxin
Intestinal bile acids directly modulate the structure and function of <i>C. difficile</i> TcdB toxin Open
Significance Clostridioides difficile is a bacterial pathogen of global importance that is a major cause of hospital-acquired diarrhea. Antibiotic-mediated disruptions to the gut microbiota and associated metabolome promote C. difficile gr…
View article: Structural and Mechanical Roles for the C-Terminal Nonrepetitive Domain Become Apparent in Recombinant Spider Aciniform Silk
Structural and Mechanical Roles for the C-Terminal Nonrepetitive Domain Become Apparent in Recombinant Spider Aciniform Silk Open
Spider aciniform (or wrapping) silk is the toughest of the seven types of spider silks/glue due to a combination of high elasticity and strength. Like most spider silk proteins (spidroins), aciniform spidroin (AcSp1) has a large core repet…
View article: Tracking Transitions in Spider Wrapping Silk Conformation and Dynamics by <sup>19</sup>F Nuclear Magnetic Resonance Spectroscopy
Tracking Transitions in Spider Wrapping Silk Conformation and Dynamics by <sup>19</sup>F Nuclear Magnetic Resonance Spectroscopy Open
Aciniform silk protein (AcSp1) is the primary component of wrapping silk, the toughest of the spider silks because of a combination of high tensile strength and extensibility. Argiope trifasciata AcSp1 contains a core repetitive domain wit…