title: Evaluation of biologically relevant short alpha-helices stabilized by a main-chain hydrogen-bond surrogate.
abstract: We previously reported the design and synthesis of a new class of artificial alpha-helices in which an N-terminal main-chain hydrogen bond is replaced by a carbon-carbon bond derived from a ring-closing metathesis reaction [Chapman, R. N.; Dimartino, G.; Arora, P. S. J. Am. Chem. Soc. 2004, 126, 12252-12253]. Our initial study utilized an alanine-rich sequence; in the present manuscript we evaluate the potential of this method for the synthesis of very short (10 residues) alpha-helices representing two different biologically relevant alpha-helical domains. We extensively characterized these two sets of artificial helices by NMR and circular dichroism spectroscopies and find that the hydrogen-bond surrogate approach can afford well-defined short alpha-helical structures from sequences that do not spontaneously form alpha-helical conformations.
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Deyun
authors.initials: D
authors.lastname: Wang
authors.forename: Kang
authors.initials: K
authors.lastname: Chen
authors.forename: John L
authors.initials: JL
authors.lastname: Kulp Iii
authors.forename: Paramjit S
authors.initials: PS
authors.lastname: Arora
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins