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. 2020 Jan 24;10:1163. doi: 10.1038/s41598-020-58305-y

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Isolation of putative receptor-binding sites of rNadA using on-membrane limited tryptic digestion (nitrocellulose membrane) (A) (1) MALDI spectrum of in-solution limited tryptic digestion (20 min digestion) of rNadA, (2) rNadA incubated with ~17 kDa receptor on nitrocellulose membrane was trypsinized, interacting peptides were stripped, acetone precipitated and identified on MALDI-TOF, (3) negative control generated by omitting tryptic digestion, (4) negative control generated by omitting rNadA from the protocol. (B) Depicts rNadA recovered after interaction with ~17 kDa receptor from nitrocellulose membrane without trypsinization and identified on MALDI-TOF. C represents list of theoretical peptides of rNadA predicted by in-silico tryptic digestion using mMass software. Peptides identified from on-membrane limited proteolysis of ligand-receptor complex (A2), matching with in-solution digestion of ligand (A1) and theoretical masses (C) are framed. Please note that predicted masses of the peptides are [M + 1 H] +. The observed masses of the peptides are also [M + 1 H] +.