Prof Chirag Dhara to share insights on education for climate action at the ‘International Conference on Sustainable Development 2021’ | Today @ 10.30 PM IST

Prof Chirag Dhara to share insights on education for climate action at the ‘International Conference on Sustainable Development 2021’ | Today @ 10.30 PM IST

Prof Chirag Dhara, Assistant Professor of Environmental Studies at Krea University, will present at the ‘International Conference on Sustainable Development 2021’ along with Prof Vandana Singh from Framingham University, USA. In line with the theme of the conference – ‘Education for Climate Action: Towards an SDG 4.7 Roadmap for Systems Change’ – their presentation (titled ‘Why Transformative Education Must Address the Problem of Endless Exponential Economic Growth’) aims to provide a conceptual scaffolding around which learning frameworks may be developed to make room for diverse alternative paths to truly sustainable social-ecological cultures. Their presentation is based on a book chapter that they have contributed to an upcoming edited volume on the same theme, to be published by UNESCO.

For more information about the conference, visit: https://ic-sd.org/

Prof Srajana Kaikini’s recent papers published by noted international journals

Prof Srajana Kaikini’s recent papers published by noted international journals

Krea faculty Prof Srajana Kaikini — Assistant Professor of Philosophy, Humanities & Social Sciences & Literature & the Arts — has had two of her recent papers published by renowned international journals. Her most recent paper explores strategies within the arts practice, while the other paper talks about COVID-19 and its social impact.

Her paper titled, ‘The Aesthetics Of Risk in Artistic Practice: What is at Stake?’, has been published in the Kunstlicht Journal 41(4) (2020). ASSESSING RISK: ON STRATEGIES FOR HEALTH, SAFETY, AND WELFARE WITHIN ARTS PRACTICE. The journal regularly features academics, authors, editors and artists sharing their insights on art, visual culture, and architecture. Access the paper here.

Her timely piece on understanding disasters and bringing the ethical language of the collective, bearing COVID-19 in mind, was published by Voices in Bioethics, an online journal in partnership with Columbia University Library. Read the article here.

Prof Kalyan Chakrabarti co-authors paper on “Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein”

Prof Kalyan Chakrabarti co-authors paper on “Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein”

Prof Kalyan Chakrabarti – Assistant Professor of Biological Science & Chemistry, Krea University – co-authors with scientists at IISc for a paper on “Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein” published in the American Chemical Society journal ‘Biochemistry’.

About the paper:

The cells are the tiny units of life. Protein molecules are the engines that carry out all the necessary work within the cell. But, how are the engines assembled within the cell?  A team of scientists, including Prof Kalyan Chakrabarti, have answered this question in an article published in the American Chemical Society journal ‘Biochemistry’. The work, partially funded by the Krea Intramural Fellowship awarded in 2019, discusses a specific problem of viral infection in plants which has the potential to provide a blueprint for preventing viral infections in animals too.

Abstract:

The plant Sesbania mosaic virus [a (+)-ssRNA sobemovirus] VPg protein is intrinsically disordered in solution. For the virus life cycle, the VPg protein is essential for replication and for polyprotein processing that is carried out by a virus-encoded protease. The nuclear magnetic resonance (NMR)-derived tertiary structure of the protease-bound VPg shows it to have a novel tertiary structure with an α-β-β-β topology. The quaternary structure of the high-affinity protease–VPg complex (≈27 kDa) has been determined using HADDOCK protocols with NMR (residual dipolar coupling, dihedral angle, and nuclear Overhauser enhancement) restraints and mutagenesis data as inputs. The geometry of the complex is in excellent agreement with long-range orientational restraints such as residual dipolar couplings and ring-current shifts. A “vein” of aromatic residues on the protease surface is pivotal for the folding of VPg via intermolecular edge-to-face π···π stacking between Trp271 and Trp368 of the protease and VPg, respectively, and for the CH···π interactions between Leu361 of VPg and Trp271 of the protease. The structure of the protease–VPg complex provides a molecular framework for predicting sites of important posttranslational modifications such as RNA linkage and phosphorylation and a better understanding of the coupled folding upon binding of intrinsically disordered proteins. The structural data presented here augment the limited structural data available on viral proteins, given their propensity for structural disorder.

Reference: Karuna Dixit, N. Megha Karanth, Smita Nair, Khushboo Kumari, Kalyan S. Chakrabarti, Handanahal S. Savithri, and Siddhartha P. Sarma | Biochemistry 2020 59 (49), 4663-4680 | DOI: 10.1021/acs.biochem.0c00721

Read the complete paper, here.