G
Gautam Basu
Researcher at Bose Institute
Publications - 83
Citations - 2060
Gautam Basu is an academic researcher from Bose Institute. The author has contributed to research in topics: Helix & Peptide. The author has an hindex of 25, co-authored 77 publications receiving 1835 citations. Previous affiliations of Gautam Basu include Japan Atomic Energy Research Institute & University of Texas Health Science Center at San Antonio.
Papers
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Journal ArticleDOI
Paramagnetic viral nanoparticles as potential high-relaxivity magnetic resonance contrast agents.
Mark Allen,Jeff W.M. Bulte,Lars O. Liepold,Gautam Basu,Holly A. Zywicke,Joseph A. Frank,Mark J. Young,Trevor Douglas +7 more
TL;DR: The preliminary results should encourage further investigations into the use of viral protein cages as a new platform for MR contrast agents and the unusually high relaxivity values of the Gd3+–CCMV are largely a result of the nanoparticle virus size and the large number of Gd 3+ ions bound to the virus.
Journal ArticleDOI
Self-assembling biomolecular catalysts for hydrogen production
Paul Jordan,Paul Jordan,Dustin P. Patterson,Kendall N. Saboda,Ethan Edwards,Ethan Edwards,Heini M. Miettinen,Gautam Basu,Megan C. Thielges,Trevor Douglas +9 more
TL;DR: This work shows the encapsulation and protection of an active hydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly through probing the infrared spectroscopic signatures and catalytic activity of the engineered material.
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Curcumin recognizes a unique binding site of tubulin.
Soumyananda Chakraborti,Lalita Das,Neha Kapoor,Amlan Das,Vishnu Dwivedi,Asim Poddar,Gopal Chakraborti,Mark E. Janik,Gautam Basu,Dulal Panda,Pinak Chakrabarti,Avadhesha Surolia,Bhabatarak Bhattacharyya +12 more
TL;DR: Using fluorescence spectroscopy, it is shown that curcumin binds tubulin 32 Å away from the colchicine-binding site, and structure-activity studies suggest that the tridented nature of compound 7 is responsible for its higher affinity for tubulin compared toCurcumin.
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Coconfinement of fluorescent proteins: spatially enforced communication of GFP and mCherry encapsulated within the P22 capsid.
TL;DR: Results indicate that FRET is sensitive to the expansion of the capsid and encapsulation enforces significant intermolecular communication, increasing FRET by 5-fold, which is a promising platform for studying crowding, enforced proximity, and confinement effects on communication between active proteins.
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Sequence and structure patterns in proteins from an analysis of the shortest helices: implications for helix nucleation.
TL;DR: An important role played by shortest 3(10)-helices in proteins with important structural and folding implications is ascribed, based on correlation matrices of site-specific amino acid composition, and the relative abundance of these short secondary structural elements.