title: Short sequences of non-proline residues can adopt the polyproline II helical conformation.
abstract: The left-handed polyproline II (P(II)) helix is a structure that has been given a great deal of attention lately because of its role in a wide variety of physiologically important processes and potential significance in protein unfolded states. Recent work by several authors has shown that residues besides proline can adopt this structure. A scale of relative P(II)-helix-forming propensities has been generated but only for single guest residues in a proline-based host system. Here, we present multiple guest residues in a proline-based host system. Using circular dichroism spectroscopy, we have shown that not only single residues, but also short sequences of non-proline residues can adopt the P(II) conformation.
authors.affiliation: Center for Structural Biology, Department of Molecular and Cellular Biochemistry, University of Kentucky, 800 Rose Street, Lexington, Kentucky 40536-0298, USA.
authors.forename: Brian W
authors.initials: BW
authors.lastname: Chellgren
authors.forename: Trevor P
authors.initials: TP
authors.lastname: Creamer
mesh_terms: D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D001216:Asparagine / Q000737:chemistry; D002942:Circular Dichroism; D005973:Glutamine / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013053:Spectrophotometry; D014633:Valine / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D010455:Peptides; D005973:Glutamine; C011083:polyproline; D001216:Asparagine; D011392:Proline; D014633:Valine; D000409:Alanine