Abstract
Many proteins contain disordered segments that play important roles in vivo. Autotransporter (AT) proteins are key virulence proteins from pathogenic Gram-negative bacteria. AT proteins have disordered properties that have been shown to be crucial for their efficient secretion to the bacterial cell surface, but much remains unknown regarding the amino acid sequence properties that dictate protein disorder. In previous work using small angle X-ray scattering (SAXS), we showed that local clustering of hydrophobic residues leads to a significant collapse of a disordered segment of the AT protein pertactin (Bowman et al., (2020) PNAS), a virulence protein from Bordetella pertussis, the bacterium that causes whooping cough.
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