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Journal Article

Ravikumar, Ashraya and Ramakrishnan, Chandrasekharan and Srinivasan, Narayanaswamy (2019) Stereochemical Assessment of (phi,psi) Outliers in Protein Structures Using Bond Geometry-Specific Ramachandran Steric-Maps. In: STRUCTURE, 27 (12). 1875+.

Crisma, Marco and Formaggio, Fernando and Aleman, Carlos and Torras, Joan and Ramakrishnan, Chandrasekharan and Kalmankar, Neha and Balaram, Padmanabhan and Toniolo, Claudio (2018) The fully-extended conformation in peptides and proteins. In: PEPTIDE SCIENCE, 110 (5, SI).

Toniolo, Claudio and Crisma, Marco and Formaggio, Fernando and Aleman, Carlos and Ramakrishnan, Chandrasekharan and Kalmankar, Neha and Balaram, Padmanabhan (2017) Intramolecular backbone center dot center dot center dot backbone hydrogen bonds in polypeptide conformations. The other way around: epsilon-turn. In: BIOPOLYMERS, 108 (1, SI).

Toniolo, Claudio and Crisma, Marco and Moretto, Alessandro and Peggion, Cristina and Formaggio, Fernando and Aleman, Carlos and Cativiela, Carlos and Ramakrishnan, Chandrasekharan and Balaram, Padmanabhan (2015) Peptide delta-Turn: Literature Survey and Recent Progress. In: CHEMISTRY-A EUROPEAN JOURNAL, 21 (40). pp. 13866-13877.

Chatterjee, Sunanda and Vasudev, Prema G and Raghothama, Srinivasarao and Ramakrishnan, Chandrasekharan and Shamala, Narayanaswamy and Balaram, Padmanabhan (2009) Expanding the Peptide beta-Turn in alpha gamma Hybrid Sequences: 12 Atom Hydrogen Bonded Helical and Hairpin Turns. In: Journal of the American Chemical Society, 131 (16). pp. 5956-5965.

Vasudev, Prema G and Chatterjee, Sunanda and Ramakrishnan, Chandrasekharan and Shamala, Narayanaswamy and Balaram, Padmanabhan (2009) Conformational Choices for the Stereochemically Constrained gamma-Amino Acid Residue Gabapentin: Theoretical Studies and Correlation With Experimental Results. In: Biopolymers, 92 (5). pp. 426-435.

Ganesh, C and Eswar, Narayanan and Srivastava, Sarika and Ramakrishnan, Chandrasekharan and Varadarajan, Raghavan (1999) Prediction of the maximal stability temperature of monomeric globular proteins solely from amino acid sequence. In: FEBS Letters, 454 (1-2). pp. 31-36.