The Perturbation of Tryptophan Fluorescence by Phenylalanine to Alanine Mutations Identifies the Hydrophobic Core in a Subset of Bacterial Ig-like Domains
2013
Raman, Rajeev | Ptak, Christopher P. | Xie, Jinglin | Oswald, Robert E. | Chang, Yung-Fu | Sharma, Yogendra
Many host–parasite interactions are mediated via surface-exposed proteins containing bacterial immunoglobulin-like (Big) domains. Here, we utilize the spectral properties of a conserved Trp to provide evidence that, along with a Phe, these residues are positioned within the hydrophobic core of a subset of Big_2 domains. The mutation of the Phe to Ala decreases Big_2 domain stability and impairs the ability of LigBCen2 to bind to the host protein, fibronectin.
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