An N-terminal half fragment of the histidine phosphocarrier protein, HPr, is disordered but binds to HPr partners and shows antibacterial properties - Neira, José L.; Palomino-Schätzlein, Martina; Hurtado-Gómez, Estefanía; Ortore, María G.; Falcó, Alberto (Biochimica et biophysica acta. General subjects, 2021)
Keywords: active sites; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - metabolism; Anti-Bacterial Agents - pharmacology; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding; carbon; Circular dichroism; circular dichroism spectroscopy; Escherichia coli - metabolism; Fluorescence; histidine; Histidine-phosphocarrier-protein; interferometry; NMR; nuclear magnetic resonance spectroscopy; Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry; Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism; phosphorylase; Protein Binding; Protein-protein interactions; serine; small-angle X-ray scattering; ultraviolet radiation; RU; Fluorescence; PPI; RNAP; PTS; EIsc; EINsc; SPR; HPrK/P; MH; Binding; FPLC; CD; UV; Rsd; SDS; EI; EII; HPrsc; MIC; PAGE; EIN; HPr; Protein-protein interactions; Circular dichroism; SAXS; NMR; HPr48; HPrK/Pbs; LB; Rsdec; PEP; HSQC; BLI; HPr9-30; SAM; Histidine-phosphocarrier-protein