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Journal of Molecular Biology|May 20, 1991
Straight-chain non-polar amino acids are good helix-formers in waterS Padmanabhan, R L BaldwinJournal of Molecular Biology|September 2, 1994
Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i, i + 4S Padmanabhan, R L BaldwinProtein Science : a Publication of the Protein Society|November 1, 1994
Tests for helix-stabilizing interactions between various nonpolar side chains in alanine-based peptidesS Padmanabhan, R L BaldwinBiochemistry|June 1, 1993
Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensitiesA Chakrabartty, T Kortemme, S Padmanabhan, et al.Journal of Molecular Biology|April 5, 1996
Helix propensities of basic amino acids increase with the length of the side-chainS Padmanabhan, E J York, J M Stewart, et al.Nature|March 15, 1990
Relative helix-forming tendencies of nonpolar amino acidsS Padmanabhan, S Marqusee, T Ridgeway, et al.Biochemistry|July 19, 1994
Helix-forming tendencies of amino acids in short (hydroxybutyl)-L-glutamine peptides: an evaluation of the contradictory results from host-guest studies and short alanine-based peptidesS Padmanabhan, E J York, L Gera, et al.Proceedings of the National Academy of Sciences of the United States of America|November 1, 1986
Temperature dependence of the hydrophobic interaction in protein foldingR L BaldwinPageof 42