1402451-05-1Relevant articles and documents
Conformational Switching in Heterochiral α,β2,3-Hybrid Peptides in Response to Solvent Polarity
Balamurugan, Dhayalan,Muraleedharan, Kannoth M.
, p. 5321 - 5325 (2015)
The ability of α,β2,3-hybrid peptides with a heterochiral backbone to exist in a helical, extended, or partially folded state depending on the solvation conditions employed was investigated. The preference was found to be directly dictated by Cα-Cβ torsions in the β-residues. α,β-Hybrid peptides with a heterochiral backbone show the ability to exist in a helical, extended, or partially folded conformation depending on the solvation conditions employed.
Unprecedented torsional preferences in trans-β2,3-amino acid residues and formation of 11-helices in α,β2,3-hybrid peptides
Balamurugan, Dhayalan,Muraleedharan, Kannoth M.
, p. 9516 - 9520 (2012/09/21)
Anti or gauche? trans-β2,3-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments. Copyright
