title: Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β(2,3)-Hybrid Peptides.
abstract: Unfolding of helical trans-β(2,3) -hybrid peptides with (α-β)n α composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα-Cβ . This is evidenced by clear change in their Cβ H signal splitting, (3)JCαH-CβH values, and sequential disappearance of i,i+2 NOEs.
authors.affiliation: Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India).
authors.forename: Dhayalan
authors.initials: D
authors.lastname: Balamurugan
authors.affiliation: Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India). mkm@iitm.ac.in.
authors.forename: Kannoth M
authors.initials: KM
authors.lastname: Muraleedharan
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D019077:Helix-Turn-Helix Motifs; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry
chemical_list: D000596:Amino Acids; D010455:Peptides; D012997:Solvents
keywords: alpha/beta-hybrid peptides; amino acids; foldamers; helix-strand hybrid; protein folding