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| S. Krishnaswamy; Abhishek Kumar. |
| Outer membrane beta-stranded porins form a diverse and complex set of proteins which allow passage of molecules across the membrane interface have been analyzed here from a biophysical and structural perspective using atomic temperature factors or B-factors. Generally atomic temperature factors of molecules from crystal structures indicate the degree of mobility or disorder seen in the crystal structure. Structures of six porins (four 16 stranded beta barrel porins and two 8 stranded beta barrel porins) were taken from the PDB for the analysis based on resolution (better than 3.0 Å) and R-factor (< 0.23). The residue distribution and mobility distribution was found to be characteristic of each of the porins. The mobility and residue... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology. |
| Ano: 2008 |
URL: http://precedings.nature.com/documents/2495/version/1 |
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| Abhishek Kumar; S Krishnaswamy. |
| Computational and statistical analysis has formed a large component of the biophysical efforts put forth to understand protein structure and function, due to the diversity and complexity of their structure. Outer membrane proteins form a diverse and complex set of proteins. Of these, porins that allow passage of molecules across the membrane interface have been analyzed here from a biophysical and structural perspective. The objective of this study is to analyze the structural organization of porins using atomic temperature factor as a parameter. Generally atomic temperature factors of molecules from crystal structures indicate the degree of mobility or disorder seen in the crystal structure. As good crystal structures have lesser possibilities of errors... |
| Tipo: Poster |
Palavras-chave: Biotechnology. |
| Ano: 2009 |
URL: http://precedings.nature.com/documents/2803/version/1 |
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| Abhishek Kumar. |
| Computational and statistical analysis has formed a large component of the biophysical efforts put forth to understand protein structure and function, due to the diversity and complexity of their structure. Outer membrane proteins form a diverse and complex set of proteins. Of these, porins which allow passage of molecules across the membrane interface have been analyzed here from a biophysical and structural perspective. The objective of this study is to analyze the structural organization of porins using atomic temperature factor as a parameter. Generally atomic temperature factors of molecules from crystal structures indicate the degree of mobility or disorder seen in the crystal structure. As good crystal structures have fewer possibilities of errors... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Microbiology; Bioinformatics. |
| Ano: 2012 |
URL: http://precedings.nature.com/documents/7016/version/1 |
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| Abhishek Kumar; Hermann Ragg. |
| The superfamily of serine proteinase inhibitors (serpins) is involved in wide arrays of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression. The average protein size of a serpin family member is 350-400 amino acids, but gene structure varies in terms of number and position of exons and introns. All known serpins can be grouped into 16 clades and 10 orphan sequences. Vertebrate serpins can be conveniently classified into six sub-groups, based on three independent biological features - genomic organization, diagnostic amino acid sites and rare indels.
The objective of this study was to elucidate the phylogenetic kinships of serpins involved in... |
| Tipo: Poster |
Palavras-chave: Bioinformatics; Evolutionary Biology. |
| Ano: 2008 |
URL: http://precedings.nature.com/documents/2496/version/1 |
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| Abhishek Kumar. |
| The superfamily of serine proteinase inhibitors (serpins) is involved in an array of fundamental biological processes such as blood coagulation, cell differentiation, cell migration, complement activation, embryo implantation, fibrinolysis, angiogenesis, and inflammation, and tumor suppression. Vertebrate serpins can be conveniently classified into six sub-groups, based on three independent biological features - genomic organization, diagnostic amino acid sites and rare indels. The present vertebrate serpins are derived from an original serpin most probably by intron insertion and we are trying to reconstruct the phylogeny of vertebrate serpin and looking for the reconstruction of original vertebrate gene(s). We started with fish genomes and characterized... |
| Tipo: Manuscript |
Palavras-chave: Genetics & Genomics; Evolutionary Biology. |
| Ano: 2009 |
URL: http://precedings.nature.com/documents/3050/version/1 |
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| Shweta Tripathi; Sumit Kumar Sonkar; Abhishek Kumar; M.Y. Khan; Sabyasachi Sarkar. |
| Multi-walled Carbon nanotube, its role and implications in biological systems are currently under evaluation and became interesting for many researchers primarily working on the interface of chemistry, physics and biology. However, concerns about the potential toxicity of multi-walled carbon nanotubes have been raised. To carry such affords, herein we investigate the effects of carboxylic acid functionalized water soluble carbon nanotube (wsCNT) on the growth of gram Cicer arietinum plant. The growth of gram plants was observed with and without the presence of wsCNT to demonstrate that carboxylated functionalized multi-walled carbon nanotubes showed better growth and under more wsCNT, the growth was enhanced without showing apparent toxicity. Although... |
| Tipo: Manuscript |
Palavras-chave: Chemistry; Plant Biology. |
| Ano: 2009 |
URL: http://precedings.nature.com/documents/4056/version/1 |
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