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6.8 years ago
olima.marx
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I am trying to use a text mining tool called NlProt, but for to do so i need to convert a set of pubmed abstracts into NlProt format, which is something like:
plain natural language text (each line = one abstract/paper)
lines have to start with number followed by ">" and then the text
e.g. 0001>abstract1 abstract1 abstract1 ...
Can anyone help me?
PS: This is an example of the pubmed abstract format
1. Biotechnol Prog. 2017 May 27. doi: 10.1002/btpr.2508. [Epub ahead of print]
Enhanced expression of cysteine-rich antimicrobial peptide snakin-1 in
Escherichia coli using an aggregation-prone protein coexpression system.
Kuddus MR(1)(2), Yamano M(1), Rumi F(1), Kikukawa T(1)(3), Demura M(1)(3), Aizawa
T(1)(3).
Author information:
(1)Graduate School of Life Science, Hokkaido University, Sapporo, Hokkaido,
060-0810, Japan.
(2)Dept. of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka,
Dhaka, 1000, Bangladesh.
(3)Global Station for Soft Matter, Global Inst. for Collaborative Research and
Education, Hokkaido University, Sapporo, Japan.
Snakin-1 (SN-1) is a cysteine-rich plant antimicrobial peptide and the first
purified member of the snakin family. SN-1 shows potent activity against a wide
range of microorganisms, and thus has great biotechnological potential as an
antimicrobial agent. Here, we produced recombinant SN-1 in Escherichia coli by a
previously developed coexpression method using an aggregation-prone partner
protein. Our goal was to increase the productivity of SN-1 via the enhanced
formation of insoluble inclusion bodies in E. coli cells. The yield of SN-1 by
the coexpression method was better than that by direct expression in E. coli
cells. After refolding and purification, we obtained several milligrams of
functionally active SN-1, the identity of which was verified by MALDI-TOF MS and
NMR studies. The purified recombinant SN-1 showed effective antimicrobial
activity against test organisms. Our studies indicate that the coexpression
method using an aggregation-prone partner protein can serve as a suitable
expression system for the efficient production of functionally active SN-1. ©
2017 American Institute of Chemical Engineers Biotechnol. Prog., 2017.
© 2017 American Institute of Chemical Engineers.
DOI: 10.1002/btpr.2508
PMID: 28556600
Hello olima.marx!
It appears that your post has been cross-posted to another site: https://stackoverflow.com/questions/44800109
This is typically not recommended as it runs the risk of annoying people in both communities.