1. Automated design evolution of stereochemically randomized protein foldamers. (1st March 2018) Authors: Ranbhor, Ranjit; Kumar, Anil; Patel, Kirti; Ramakrishnan, Vibin; Durani, Susheel Journal: Physical biology Issue: Volume 15:Number 3(2018:Jun.) Page Start: Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
2. Automated protein design: Landmarks and operational principles. (May 2017) Authors: Kumar, Anil; Ranbhor, Ranjit; Patel, Kirti; Ramakrishnan, Vibin; Durani, Susheel Journal: Progress in biophysics and molecular biology Issue: Volume 125(2017) Page Start: 24 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
3. Biomimetic design: a programmed tetradecapeptide folds and auto-dimerizes as a stereochemically articulated receptor protein. Issue 8 (14th January 2016) Authors: Ghosh, Punam; Pednekar, Deepa; Durani, Susheel Journal: RSC advances Issue: Volume 6:Issue 8(2016) Page Start: 6077 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
4. Computational scrutiny of the effect of N-terminal proline and residue stereochemistry in the nucleation of α-helix fold. Issue 78 (4th August 2016) Authors: Goyal, Bhupesh; Kumar, Anil; Srivastava, Kinshuk Raj; Durani, Susheel Journal: RSC advances Issue: Volume 6:Issue 78(2016) Page Start: 74162 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
5. De novo design of stereochemically-bent sixteen-residue β-hairpin as a hydrolase mimic. Issue 127 (14th December 2015) Authors: Goyal, Bhupesh; Patel, Kirti; Srivastava, Kinshuk Raj; Durani, Susheel Journal: RSC advances Issue: Volume 5:Issue 127(2015) Page Start: 105400 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
6. Examination of the Effect of N‐terminal Diproline and Charged Side Chains on the Stabilization of Helical Conformation in Alanine–based Short Peptides: A Molecular Dynamics Study. Issue 19 (1st December 2016) Authors: Goyal, Bhupesh; Srivastava, Kinshuk Raj; Durani, Susheel Journal: ChemistrySelect Issue: Volume 1:Issue 19(2016) Page Start: 6321 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
7. IDeAS: automated design tool for hetero-chiral protein folds. (14th August 2018) Authors: Ranbhor, Ranjit; Kumar, Anil; Tendulkar, Abhijit; Patel, Kirti; Ramakrishnan, Vibin; Durani, Susheel Journal: Physical biology Issue: Volume 15:Number 6(2018:Dec.) Page Start: Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
8. Modulation of β‐Hairpin Peptide Self‐Assembly: A Twenty‐Residue Poly‐l β‐Hairpin Modified Rationally as a Mixed‐l, d Hydrolase. Issue 9 (27th June 2016) Authors: Goyal , Bhupesh; Srivastava , Kinshuk Raj; Patel , Kirti; Durani, Susheel Journal: ChemistrySelect Issue: Volume 1:Issue 9(2016) Page Start: 2050 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
9. N‐terminal diproline and charge group effects on the stabilization of helical conformation in alanine‐based short peptides: CD studies with water and methanol as solvent. (20th April 2017) Authors: Goyal, Bhupesh; Srivastava, Kinshuk Raj; Durani, Susheel Journal: Journal of peptide science Issue: Volume 23:Number 6(2017) Page Start: 431 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗
10. Probing the role of electrostatics of polypeptide main-chain in protein folding by perturbing N-terminal residue stereochemistry: DFT study with oligoalanine models. Issue 114 (6th December 2016) Authors: Goyal, Bhupesh; Srivastava, Kinshuk Raj; Kumar, Anil; Patwari, G. Naresh; Durani, Susheel Journal: RSC advances Issue: Volume 6:Issue 114(2016) Page Start: 113611 Record Type: Journal Article View Content: Available online (eLD content is only available in our Reading Rooms) ↗