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Search Results: 1 - 10 of 507816 matches for " RAJASEKARAN E and VIJAYASARATHY M "
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International Journal of Bioinformatics Research , 2011,
Abstract: Alanine aminotransferase (ALT) is an enzymatic protein involved in catabolism of amino acids. The carbondistribution study on this clinically important protein is carried out here. The study reveals that the carbon content is generallyhigher than the expected values of 31.45%. The alteration in carbon content other than the active site might improve theactivity of this enzymatic protein. Particularly the reduction at the carboxyl end of the sequence is more appropriate. Carbondistribution analysis clearly locates the active site of ALT protein, which is reported here.
CARBANA: Carbon analysis program for protein sequences
Ekambaram Rajasekaran,Marimuthu Vijayasarathy
Bioinformation , 2011,
Abstract: There are lots of works gone into proteins to understand the nature of proteins. Hydrophobic interaction is the dominant force that drives the proteins to carry out the biochemical reactions in all living system. Carbon is the only element that contributes towards this hydrophobic interaction. Studies find that globular proteins prefer to have 31.45% of carbon for its stability. Taking this as standard, a carbon analysis program has been developed to study the carbon distribution profile of protein sequences. This carbon analysis program has been made available online. This can be accessed at www.rajasekaran.net.in/tools/carbana.html. This new program is hoped to help in identification and development of active sites, study of protein stability, evolutionary understating of proteins, gene identification, ligand binding site identification, and to solve the long-standing problem of protein-protein and protein-DNA interactions.
Allotment of carbon is responsible for disorders in proteins
Ekambaram Rajasekaran,Kannaiyan Akila,Marimuthu Vijayasarathy
Bioinformation , 2011,
Abstract: Sequence stretches in proteins that do not fold into a form are referred as disordered regions. Databases like Disport describe disordered regions in proteins and web servers like PrDOS and DisEMBL, facilitate the prediction of disordered regions. These studies are often based on residue level features. Here, we describe proteins with disordered regions using carbon content and distributions. The distribution pattern for proteins with disordered regions is different from those that do not show disordered regions.
Compositional analysis of protein sequences of different species
Vinobha C.S.,Rajasekaran E.,Rajadurai M.
International Journal of Bioinformatics Research , 2010,
Abstract: We describe several protein sequence statistics designed to evaluate distinctive attributes ofresidue content and arrangement in primary structure. As per the global consideration, thecompositional biases of clustering different residue types (charged residues, hydrophobic residues) oflong runs of charged or uncharged residues, periodic patterns, counts and distribution ofhomooligopeptides, and unusual spacing between particular residue types. The computer programSEQUANA (statistical analysis of protein sequences) calculates all the statistics for any individualprotein sequence input and is available for the WINDOWS environment through electronic mail onrequest to csvinobha@gmail.com
Carbon Distribution in Protein Structure Might Influences Thermostability of Modified Form
Rajasekaran E.
Advanced Biotech , 2013,
Abstract: Hydrophobic interaction is the dominant force in proteins that arises from carbon. The carbon content and distribution make a protein to fold in form to have stability and function. The science of carbon in toxic protein, thermolabile protective antigen in native and mutant form is studied. The CARd analysis program is used for this purpose. The results reveal that carbon distribution in local structure is responsible for thermolability. The CARd analysis is able explain this phenomena of protein stabilisation. It also suggests that before going for protein engineering, this simple carbon distribution study can be performed for validation. This can be utilised for production of stable proteins.
The nature of proteins in influenza  [PDF]
K. Akila, P. Balamurugan, E. Rajasekaran
Health (Health) , 2012, DOI: 10.4236/health.2012.430151
Abstract: Mutation can alter the structure of viral proteins to form different structure. Carbon distribution is responsible for these changes in structure. The carbon distribution in proteins of human Influenza A virus is analyzed here. Results reveal that the carbon contents are high in surface proteins, optimum in polymerase proteins and less in nuclear proteins. Polymerase proteins have better carbon distribution pattern than the other proteins. Thymine distribution in different frames of mRNAs are checked as it has link with carbon distribution pattern in the corresponding proteins. Results show that frame 4 is violating from thymine distribution. This is responsible for production of protein with different carbon distribution. Unusual thymine distribution in frame 3 are observed. The thymine distributions are different in viral mRNA compared to normal one. Minimizing the excess thymine in H1N1 mRNAs might improve the protein performance. Mutational study based on carbon distribution should be better exploited for further improving the protein stability, activity and ultimately for gene therapy.
What Might be the Difference in Viral Proteins?
Akila K.,Rajasekaran E.
International Journal of Bioinformatics Research , 2009,
Abstract: The difference between normal and viral proteins is the way the amino acids organized in someform. Though both proteins use same 20 naturally occurring amino acids, it differs in arrangements. Thisdifference cannot be felt by merely comparing the amino acid sequence but at atom level. This is analysedand compared in terms of carbon distribution as carbon is the only element that contributes towards thedominant force, hydrophobic interaction. For this purpose the arenaviruses have been selected here forstudy. The protein sequences of 7 arenaviruses are analysed. Our results show that the carbon distributionin viral proteins is different from the normal proteins. Either the carbon content is different or the distributionis not uniform. This carbon distribution analysis uses our earlier report of 31.44% of carbon for its structureand activity.
Cardioprotective Effect of a Medicinal Mushroom, Ganoderma lucidum Against Adriamycin Induced Toxicity
M. Rajasekaran,C. Kalaimagal
International Journal of Pharmacology , 2012,
Abstract: The present study was conducted to evaluate the cardioprotective role of a medicinal mushroom, Ganoderma lucidum against the toxicity of an anticancer drug adriamycin. Wistar rats were administered with adriamycin (1.5 mg kg-1 b.wt.) for three weeks to induce cardiotoxicity. Another group was treated with adriamycin and Ganoderma extract (250 mg kg-1) for 30 days. Adriamycin treatment resulted in increased serum levels of marker enzymes such as alanine amino transferase (ALT), aspartate amino transferase (AST), lactate dehydrogenase (LDH) and creatine kinase (CK). Besides increasing the lipid peroxidation (LPO), adriamycin significantly reduced antioxidant enzymes, glutathione peroxidase (GPx), glutathione-S-transferase (GST), superoxide dismutase (SOD) and catalase (CAT) in the heart tissue. Level of reduced glutathione (GSH) was also significantly reduced. However, in G. lucidum extract treated rats the alterations were not significant, but found to be nearer to the control. The study shows that G. lucidum extract exhibits significant antioxidant property and protect the heart from free radical mediated toxicity of adriamycin.
Rajasekaran E.,Asha Jacob,Klaus Heese
International Journal of Bioinformatics Research , 2012,
Abstract: Thymine is the one and only base transcribed into uracil during production of proteins. Thymine in DNA and uracil in mRNA plays a major role in producing proteins with appropriate carbon content for stability and activity. Thymine distribution is different frames of coding nucleic acids are investigated statistically. The results confirm that frame 1 supposed to have definite thymine content. Frame 3 prefers to have least thymine content. Frames 4 & 5 maintain some degree of thymine while 2 & 6 have a variable fraction of thymine
Effects of Single Nucleotide Polymorphisms on Human N-Acetyltransferase 2 Structure and Dynamics by Molecular Dynamics Simulation
M. Rajasekaran,Santhanam Abirami,Chinpan Chen
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0025801
Abstract: Arylamine N-acetyltransferase 2 (NAT2) is an important catalytic enzyme that metabolizes the carcinogenic arylamines, hydrazine drugs and chemicals. This enzyme is highly polymorphic in different human populations. Several polymorphisms of NAT2, including the single amino acid substitutions R64Q, I114T, D122N, L137F, Q145P, R197Q, and G286E, are classified as slow acetylators, whereas the wild-type NAT2 is classified as a fast acetylator. The slow acetylators are often associated with drug toxicity and efficacy as well as cancer susceptibility. The biological functions of these 7 mutations have previously been characterized, but the structural basis behind the reduced catalytic activity and reduced protein level is not clear.
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