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Suparna Sanyal

Researcher at Uppsala University

Publications -  91
Citations -  2752

Suparna Sanyal is an academic researcher from Uppsala University. The author has contributed to research in topics: Ribosome & Ribosomal RNA. The author has an hindex of 29, co-authored 86 publications receiving 2348 citations. Previous affiliations of Suparna Sanyal include Max Planck Society & University of Calcutta.

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Interaction of Nucleobases and Aromatic Amino Acids with Graphene Oxide and Graphene Flakes

TL;DR: In this article, the authors have studied the interactions of nucleobases and aromatic amino acids with graphene and graphene oxide flakes by ab initio density functional theory (DFT) and showed that the results are consistent with the results of the previous work.
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RF3 Induces Ribosomal Conformational Changes Responsible for Dissociation of Class I Release Factors

TL;DR: The crystal structure of E. coli RF3*GDP is presented, which has a three-domain architecture strikingly similar to the structure of EF-Tu*GTP, which shows that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3.
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The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain.

TL;DR: Heteronuclear NMR spectroscopy is demonstrated that L12 binds directly to the factors IF2,EF-Tu, EF-G, and RF3 from Escherichia coli, and the region of L12 involved in these interactions is mapped, indicating that the L12-factor complexes will be highly populated on the ribosome, because of the high local concentration of ribosomes-bound factor with respect to L12.
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Structural and functional insights into the mode of action of a universally conserved Obg GTPase.

TL;DR: Kinetics and cryo-electronmicroscopy data provide insights into GTPase ObgE's role as a ribosome anti-association factor that is modulated by nutrient availability, coupling growth control to ribosomes biosynthesis and protein translation.
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The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structure.

TL;DR: Small-angle X-ray scattering data from E. coli RF1 and from a functionally active truncated RF1 derivative obviate the need for assuming large conformational changes in RFs during termination.