pone.0218507.g001.tif (475.48 kB)
The original bNK2A-C10C20 and an analog bNK2A-S10S20 peptides showed similar α-helical confirmations.
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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. ReinhardtCircular dichroism (CD) spectral analysis of the peptides (20 μM final concentrations) was performed at room temperature using Jasco J-850 CD spectrophotometer in the presence of or absence of 50% TFE. Measurements were taken every 0.1 nm from 200 nm to 250 nm. Shown graphs are the means of six accumulations after baseline correction for each peptide.
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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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