pone.0218507.g002.tif (798.26 kB)
MALDI-TOP mass spectrum analysis revealed the lack of disulfide bond formation in bNK2A-C10C20 peptide.
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posted on 2019-06-19, 17:37 authored by Rohana P. Dassanayake, Shollie M. Falkenberg, Eric M. Nicholson, Robert E. Briggs, Fred M. Tatum, Vijay K. Sharma, Timothy A. ReinhardtThe original bNK2A-C10C20 peptide incubated with PBS (A), PBS followed by IAA (B), or TCEP followed by IAA at room temperature for 60 min and molecular masses of the peptide in each sample were analyzed using Q Exactive Hybrid Quadrupole-Orbitrap Mass Spectrometer.
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well-conserved cysteine residuesbNK 2A antimicrobial activity30- mer bNK 2A peptidesintra-chain disulfide bondsbNK 2A peptideMature NK-lysin proteinbactericidal activity Bovine NK-lysinsdisulfide bondsbNK 2A forms disulfide bondsα- helical structuresNK-lysin-derived peptides show antimicrobial activityNK-lysin-derived peptidecationic antimicrobial proteins
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