‘Krea Lecture Series: Environmental Studies’ with Dr R Brawin Kumar | 28 Sept, 6.30 PM IST

‘Krea Lecture Series: Environmental Studies’ with Dr R Brawin Kumar | 28 Sept, 6.30 PM IST

In the world of mammals inhabiting the Indian subcontinent, the Madras Hedgehog is very poorly studied. Did you know that, unlike porcupines, the hedgehog’s spines are not easily detachable, and it rolls its fur-clad face and abdomen into a complete ball of spines in defence?  

Join Dr R Brawin Kumar (National Post Doctoral Fellow – School of Biology, IISER Tirupati) for an insightful and ‘edgy’ lecture — titled “The untold story of my spiny neighbour – The Madras Hedgehog!” — exploring the few species of hedgehogs in India, sharing interesting facts about them, and explaining why efforts need to be doubled towards studying these fascinating creatures.

The ‘Krea Lecture Series: Environmental Studies’ is a forum to share research and ongoing work in the broad domain of environmental issues and climate change. The series invites speakers to explore these themes from multiple dimensions including but not limited to climate science, conservation, policy, culture, social movements and more. 

This lecture is open to all. Register here: https://krea-edu-in.zoom.us/meeting/register/tJMscu-gpzooGtRWQu3ulqF1OmZPFSrnPqgm

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.