1. Capping β‐hairpin with N‐terminal d‐amino acid stabilizes peptide scaffold. Issue 3 (May 2016) Authors: Makwana, Kamlesh M.; Mahalakshmi, Radhakrishnan Journal: Biopolymers Issue: Volume 106:Issue 3(2016) Page Start: 260 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
2. Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans. Issue 2 (2nd December 2014) Authors: Gupta, Ankit; Iyer, Bharat Ramasubramanian; Chaturvedi, Deepti; Maurya, Svetlana Rajkumar; Mahalakshmi, Radhakrishnan Journal: RSC advances Issue: Volume 5:Issue 2(2015) Page Start: 1227 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
3. De novo design of metal‐binding cleft in a Trp‐Trp stapled thermostable β‐hairpin peptide. Issue 6 (18th August 2021) Authors: Lella, Muralikrishna; Mahalakshmi, Radhakrishnan Journal: Peptide science Issue: Volume 113:Issue 6(2021) Page Start: n/a Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
4. Implications of aromatic–aromatic interactions: From protein structures to peptide models. (7th October 2015) Authors: Madhusudan Makwana, Kamlesh; Mahalakshmi, Radhakrishnan Journal: Protein science Issue: Volume 24:Number 12(2015:Dec.) Page Start: 1920 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
5. Interplay of protein primary sequence, lipid membrane, and chaperone in β‐barrel assembly. (16th January 2021) Authors: Tiwari, Pankaj B.; Mahalakshmi, Radhakrishnan Journal: Protein science Issue: Volume 30:Number 3(2021) Page Start: 624 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
6. Solvation driven conformational transitions in the second transmembrane domain of mycobacteriophage holin. Issue 1 (January 2017) Authors: Lella, Muralikrishna; Mahalakshmi, Radhakrishnan Other Names: Toniolo Claudio guestEditor.; Ganesh Krishna guestEditor.; Gopi Hosahudya guestEditor.; Balaram P. guestEditor. Journal: Biopolymers Issue: Volume 108:Issue 1(2017) Page Start: n/a Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
7. Solvation driven conformational transitions in the second transmembrane domain of mycobacteriophage holin. Issue 1 (29th January 2017) Authors: Lella, Muralikrishna; Mahalakshmi, Radhakrishnan Other Names: Toniolo Claudio guestEditor.; Ganesh Krishna guestEditor.; Gopi Hosahudya guestEditor.; Balaram P. guestEditor. Journal: Biopolymers Issue: Volume 108:Issue 1(2017) Page Start: n/a Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
8. Nature of aryl–tyrosine interactions contribute to β-hairpin scaffold stability: NMR evidence for alternate ring geometry. Issue 6 (8th January 2015) Authors: Makwana, Kamlesh Madhusudan; Mahalakshmi, Radhakrishnan Journal: Physical chemistry chemical physics Issue: Volume 17:Issue 6(2015) Page Start: 4220 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
9. VDAC‐2: Mitochondrial outer membrane regulator masquerading as a channel?. (13th January 2016) Authors: Maurya, Svetlana Rajkumar; Mahalakshmi, Radhakrishnan Journal: FEBS journal Issue: Volume 283:Number 10(2016) Page Start: 1831 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
10. Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities. (7th November 2016) Authors: Maurya, Svetlana Rajkumar; Mahalakshmi, Radhakrishnan Journal: Biological reviews Issue: Volume 92:Number 4(2017:Nov.) Page Start: 1843 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗