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Bandera de FRANCE
bordeaux, france
Aquí son las 12:21 p. m.
Se unió el octubre 5, 2014
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Kashyap M.

@vaidyamkashyap

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bordeaux, france
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Scientific writing and editing

I am a talented scientific writer and editor with years of experience and educational training. My expertise lies in the area of biological sciences, considering broadly. Needless to say, I am a professional, and my work is to highest standard. Also, my expertise in this area evidenced from the high quality research papers I published in the last 8 years.

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Experiencia

Researcher

CNRS
ago 2016 - Presente
My postdoctoral research work is centered on structural classification of novel fibronectin scaffolds that specifically target post synaptic density protein-95 (PSD-95) involved in excitatory synapses in neurons.

Ph. D. researcher

UNDP
may 2008 - ago 2016 (8 años, 3 meses)
My Ph. D. thesis was centered on understanding base recognition and discrimination mechanisms of RNA binding proteins involved in alternative splicing in humans. Additionally, through a series of collaborative projects, I was involved in structural classification of bio-medically important proteins and protein complexes.

Publicaciones

1H, 13C and 15N NMR assignment of RRMs of BRUNOL-3 protein from human involved in myotonic dystrophy

Biomolecular NMR assignments/Springer
BRUNOL-3 protein, an alternate splicing factor, has been known for playing a major role in myotonic dystrophy. It binds to the cTNT m-RNA and prevents splicing of exon-5 region, leading to translation of troponin protein having differential affinity for Ca2+. Here, we report sequence-specific 1H, 13C, and 15N resonance assignments for RNA recognition motifs 1 and 2 of BRUNOL-3 protein.

Structural delineation of histone post-translation modifications in histone-NAP complex.

Journal of structural biology /Springer
Nucleosome assembly proteins (Nap) are histone chaperones with vital roles in chromatin assembly and disassembly. Decoding of histone post-translational modifications by histone chaperones is central in regulation of gene expression. We probed binding interfaces in

1H, 13C and 15N NMR assignments of inactive form of P1 endolysin Lyz

Biomolecular NMR assignments/ Springer
Lysozyme (Lyz) encoded by phage P1 is required for host cell lysis upon infection. Lyz has a N-terminal Signal Anchor Release (SAR) domain, responsible for its secretion into the periplasm and for its accumulation in a membrane tethered inactive form.

Cloning, purification, crystallization and preliminary X-ray diffraction studies EcpD.

Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Many Gram-negative bacteria are characterized by hair-like proteinaceous appendages on their surface known as fimbriae. In uropathogenic strains of Escherichia coli, fimbriae mediate attachment by binding to receptors on the host cell, often contributing to virulence

Towards solution structure and dynamics of bio-medically important membrane proteins.

International Journal of Advanced Biotechnology and Bioinformatics
Traditionally, membrane proteins have been attractive targets for therapeutics. Over 40% of all the currently available drugs in the market target membrane proteins. Therefore, basic structure-function understanding of OMPs and their complexes could

Structural characterization of the RNA binding domain of human stem loop binding protein.

International Science Press
A gene encoding the RNA binding domain (RBD) of human stem loop binding protein (SLBP) wascloned in pET 28a vector and over-expressed in E. coli codon plus cells. The over-expressed SLBP-RBD carried no tag and aggregated as inclusion bodies in the

Purification, crystallization and preliminary crystallographic studies human ETR-3.

Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The crystals diffracted to 3 Å resolution at the home source and belonged to space group P213, with unit-cell parameters a = b = c = 118.5 Å, [alpha] = [beta] = [gamma] = 90°. There were two molecules of RRM-3 in the asymmetric unit and the calculated Matthews coefficient (VM) was 6.35 Å3 Da-1, with a solvent content of 80.62%. Initial phases were determined by molecular replacement.

Sequence-specific resonance assignments of human TAF15-RRM and TAF15-RRM-RanBP2

Biomolecular NMR assignments
Human TATA binding protein associated factor 2 N (TAF15) is a RNA/DNA binding protein involved in many aspects of RNA and DNA metabolism. TAF15 contains an N-terminal transcriptional activation domain and C-terminal region comprising the RNA recognition motif (RRM) and RanBP2 type zinc finger domains with interspersed RGG motifs. In this study we report the complete backbone and side chain resonance assignments of human TAF15-RRM and backbone assignments of TAF15-RRM-RanBP2.

Structural delineation of stem-loop RNA binding by human TAF15 protein

NPG
We have compared the binding affinities across a set of single-stranded RNA oligonucleotides to conclusively establish that RNA binding is dependent upon structural elements in the RNA rather than sequence.

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