A Novel Ammonic Conversion Algorithm for Securing Data in DNA Using Parabolic Encryption

2018 ◽  
pp. 846-855
Author(s):  
Shipra Jain ◽  
Vishal Bhatnagar
Keyword(s):  
Amino Acid ◽  
Dna Sequence ◽  
Personal Data ◽  
Number System ◽  
Open Environment ◽  
Reverse Conversion ◽  
Conversion Algorithm ◽  
Dna Cryptography ◽  
Circular Arrangement ◽  
Biological Methods

In today's era, the traditional cryptographic methods are not sufficient to provide security to the data. Everyone wants to secure their data whether the data is bank transaction, email transaction, personal data or the data related to work. To provide security to the data, DNA cryptography emerges as a new field. DNA cryptography is a new branch of cryptography. It provides security to the data by converting the data in the form of DNA sequence. A lot of research has been done in the area of this cryptography. It consists of various stages like converting data in the form of DNA, reverse conversion, various methods of encryption etc. Various methods of encryption are present until now in the DNA cryptography. But the problem with them is that they all have more emphasis on biological encryption methods. There is a need of methods which make use of simple biological methods and complex binary or other number system encryption. In this paper, the authors are proposing a new algorithm for providing security to the data at two levels. The authors propose a parabolic transposition in a circular arrangement of data. In the proposed algorithm, data is arranged in a circular way. The number of rows and columns acts as a key for binary encryption. For encrypting the DNA sequence, the authors convert the DNA sequence into amino acid. This amino acid sequence will act as a cipher text and send to the receiver through the open environment. The proposed algorithm is a type of block cipher. It is a transposition cipher. It changes the position of data for binary encryption.

A Novel Ammonic Conversion Algorithm for Securing Data in DNA using Parabolic Encryption

2015 ◽  
Vol 28 (2) ◽  
pp. 20-31 ◽  
Author(s):  
Shipra Jain ◽  
Vishal Bhatnagar
Keyword(s):  
Amino Acid ◽  
Dna Sequence ◽  
Block Cipher ◽  
Personal Data ◽  
Number System ◽  
Cipher Text ◽  
Reverse Conversion ◽  
Dna Cryptography ◽  
Circular Arrangement ◽  
Biological Methods

In today's era, the traditional cryptographic methods are not sufficient to provide security to the data. Everyone wants to secure their data whether the data is bank transaction, email transaction, personal data or the data related to work. To provide security to the data, DNA cryptography emerges as a new field. DNA cryptography is a new branch of cryptography. It provides security to the data by converting the data in the form of DNA sequence. A lot of research has been done in the area of this cryptography. It consists of various stages like converting data in the form of DNA, reverse conversion, various methods of encryption etc. Various methods of encryption are present until now in the DNA cryptography. But the problem with them is that they all have more emphasis on biological encryption methods. There is a need of methods which make use of simple biological methods and complex binary or other number system encryption. In this paper, the authors are proposing a new algorithm for providing security to the data at two levels. The authors propose a parabolic transposition in a circular arrangement of data. In the proposed algorithm, data is arranged in a circular way. The number of rows and columns acts as a key for binary encryption. For encrypting the DNA sequence, the authors convert the DNA sequence into amino acid. This amino acid sequence will act as a cipher text and send to the receiver through the open environment. The proposed algorithm is a type of block cipher. It is a transposition cipher. It changes the position of data for binary encryption.

scholarly journals RNS Bases in Computer Architecture for DNA Sequence Application

2020 ◽  
Vol 9 (07) ◽  
pp. 25116-25124
Author(s):  
L.O. Olatunbosun ◽  
A.A. Adam ◽  
K.A. Gbolagade
Keyword(s):  
Computer Architecture ◽  
Dna Sequence ◽  
Gene Sequence ◽  
Chinese Remainder Theorem ◽  
Data Conversion ◽  
Future Research ◽  
Reverse Conversion ◽  
Conversion Algorithm ◽  
Arithmetic Algorithm ◽  
Open Issues

In this paper we present an RNS algorithm and architecture implementation of gene sequence applications based on an existing RNS arithmetic algorithm. Investigation was made on RNS application and its inherent arithmetic advantages; data conversion algorithm from Decimal/Binary to RNS; the forward conversion; Conversion from RNS to Binary/Decimal; the reverse conversion using the Chinese remainder theorem CRT, conversion from RNS to mixed radix form with capability for effective computation performance, and analysis of Smith Waterman Algorithm based on DNA sequence computing. Its limitations and open issues for future research were highlighted.

scholarly journals Typing of SHV Extended-Spectrum β-Lactamases by Pyrosequencing in Klebsiella pneumoniae Strains with Chromosomal SHV β-Lactamase

2008 ◽  
Vol 52 (7) ◽  
pp. 2632-2635 ◽  
Author(s):  
Marjo Haanperä ◽  
Sofia D. Forssten ◽  
Pentti Huovinen ◽  
Jari Jalava
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Dna Sequence ◽  
Reliable Method ◽  
Molecular Detection ◽  
Beta Lactamases ◽  
Extended Spectrum

ABSTRACT In Klebsiella pneumoniae, the cooccurrence of chromosomal and plasmid-mediated beta-lactamases can hinder their accurate molecular detection. We developed a fast and reliable method that allows the typing of isolates carrying more than one SHV gene. The method is based on pyrosequencing the DNA sequence corresponding to amino acid positions 35, 238, and 240.

scholarly journals DNA sequence of the E.coli trpR gene and prediction of the amino acid sequence of Trp repressor

1980 ◽  
Vol 8 (7) ◽  
pp. 1551-1560 ◽  
Author(s):  
C.K. Singleton ◽  
W.D. Roeder ◽  
Gregg Bogosian ◽  
R.L. Somerville ◽  
H.L. Weith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequence ◽  
Trp Repressor

Cloning, expression, and sequence analysis of a cytolytic enterotoxin gene from Aeromonas hydrophila

1993 ◽  
Vol 39 (5) ◽  
pp. 513-523 ◽  
Author(s):  
Ashok K. Chopra ◽  
Clifford W. Houston ◽  
Johnny W. Peterson ◽  
Gui-F. Jin
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Dna Sequence ◽  
Aeromonas Hydrophila ◽  
Biological Activities ◽  
Chinese Hamster Ovary Cells ◽  
Sodium Dodecyl ◽  
Leader Peptide ◽  
Species Variation ◽  
Enterotoxin Gene

The structural gene and regulatory element for a cytolytic enterotoxin of a diarrheal isolate, SSU, of Aeromonas hydrophila was cloned and its DNA sequence was determined. A complementary, mixed synthetic oligonucleotide based on the first 10 NH2-terminal amino acid residues of the Aeromonas cytolytic enterotoxin was used as a probe to screen a genomic library constructed in bacteriophage EMBL3. Cell lysates of Escherichia coli (λCH4), containing the cytolytic enterotoxin gene, lysed rabbit red blood cells and destroyed Chinese hamster ovary cells, caused fluid secretion in rat ileal loops, and were lethal to mice when injected intravenously. All biological activities associated with the cytolytic enterotoxin were neutralized by rabbit homologous polyclonal antibodies. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and subsequent Western blot analysis of the cell lysate of E. coli (λCH4) revealed a protein band of approximately 52 kDa, using antisera to the cytolytic enterotoxin or antibodies generated against a synthetic peptide to the toxin. DNA sequence analysis of a 2.8-kb SalI-BamHI fragment revealed the presence of one large open reading frame (1479 bp) that would encode a protein of 54.5 kDa, a precursor form of the cytolytic enterotoxin, with a 23 amino acid leader peptide. Despite a significant amount of homology at the DNA and amino acid levels between our cytolytic enterotoxin and two aerolysins of Aeromonas species, variation in the restriction maps of these three toxin genes was prominent. Likewise, considerable divergence in DNA sequence was observed upstream of the structural genes for the reported aerolysins and our cytolytic enterotoxin, suggesting that these structurally similar toxin molecules may be regulated differently. Finally, our data showed that the cytolytic enterotoxin from a diarrheal isolate, SSU, of A. hydrophila exhibited characteristics that were unique compared with those of the reported aerolysins.Key words: Aeromonas hydrophila, cytolytic enterotoxin, aerolysin, cholera toxin.

Molecular dissection of membrane-transport proteins: mass spectrometry and sequence determination of the galactose–H+ symport protein, GalP, of Escherichia coli and quantitative assay of the incorporation of [ring-2-13C]histidine and 15NH3

2002 ◽  
Vol 363 (2) ◽  
pp. 243-252 ◽  
Author(s):  
Henrietta VENTER ◽  
Alison E. ASHCROFT ◽  
Jeffrey N. KEEN ◽  
Peter J.F. HENDERSON ◽  
Richard B. HERBERT
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Membrane Transport ◽  
Dna Sequence ◽  
Transport Proteins ◽  
Tandem Ms ◽  
Esi Ms ◽  
Membrane Transport Proteins ◽  
Ms Analysis

The molecular mass of the galactose—H+ symport protein GalP, as its histidine-tagged derivative GalP(His)6, has been determined by electrospray MS (ESI-MS) with an error of <0.02%. One methionine residue, predicted to be present from the DNA sequence, was deduced to be absent. This is a significant advance on the estimation of the molecular masses of membrane-transport proteins by SDS/PAGE, where there is a consistent under-estimation of the true molecular mass due to anomalous electrophoretic migration. Addition of a size-exclusion chromatography step after Ni2+-nitrilotriacetate affinity purification was essential to obtain GalP(His)6 suitable for ESI-MS. Controlled trypsin, trypsin+chymotrypsin and CNBr digestion of the protein yielded peptide fragments suitable for ESI-MS and tandem MS analysis, and accurate mass determination of the derived fragments resulted in identification of 82% of the GalP(His)6 protein. Tandem MS analysis of selected peptides then afforded 49% of the actual amino acid sequence of the protein; the absence of the N-terminal methionine was confirmed. Matrix-assisted laser-desorption ionization MS allowed identification of one peptide that was not detected by ESI-MS. All the protein/peptide mass and sequence determinations were in accord with the predictions of amino acid sequence deduced from the DNA sequence of the galP gene. [ring-2-13C]Histidine was incorporated into GalP(His)6in vivo, and ESI-MS analysis enabled the measurement of a high (80%) and specific incorporation of label into the histidine residues in the protein. MS could also be used to confirm the labelling of the protein by 15NH3 (93% enrichment) and [19F]tryptophan (83% enrichment). Such MS measurements will serve in the future analysis of the structures of membrane-transport proteins by NMR, and of their topology by indirect techniques.

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