S
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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Journal ArticleDOI
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
Haixiao Gao,Zhi-Hong Zhou,U. Rawat,Chenhui Huang,Lamine Bouakaz,Chernhoe Wang,Zhihong Cheng,Yuying Liu,A. Zavialov,Richard Gursky,Suparna Sanyal,Måns Ehrenberg,Joachim Frank,Joachim Frank,Haiwei Song,Haiwei Song +15 more
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.
Magnus Helgstrand,Chandra Sekhar Mandava,Frans A. A. Mulder,Anders Liljas,Suparna Sanyal,Mikael Akke +5 more
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.
Boya Feng,Chandra Sekhar Mandava,Qiang Guo,Jie Wang,Wei Cao,Ningning Li,Yixiao Zhang,Yanqing Zhang,Zhi-Xin Wang,Jia-Wei Wu,Suparna Sanyal,Jianlin Lei,Ning Gao +12 more
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.
Bente Vestergaard,Suparna Sanyal,Manfred Roessle,Liliana Mora,Richard H. Buckingham,Jette S. Kastrup,Michael Gajhede,Dmitri I. Svergun,Måns Ehrenberg +8 more
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.