title: Intermediates stabilized by tryptophan pairs exist in trpzip Beta-hairpins.
abstract: Transitions of protein secondary structures, such as alpha-helices and beta-hairpins, are often too small and too fast to follow by many single-molecular approaches. Here we describe new population deconvolution methods to investigate the mechanical unfolding/refolding events in Trpzip β-hairpins that are tethered between two optically trapped polystyrene particles through click chemistry. The application of force to the Trpzip peptides shifted population distribution, which allowed us to identify intermediates from regular force-extension curves of the peptides after population deconvolution analysis. Comparison of the intermediates between the Trpzip2 and Trpzip4 peptides suggests the intermediates are likely stabilized by the tryptophan pair stacking. We anticipate the method of population deconvolution described here can offer a unique capability to investigate fast transitions in small biological structures.
authors.affiliation: Department of Chemistry and Biochemistry, Kent State University , Kent, Ohio 44242, United States.
authors.forename: Zhongbo
authors.initials: Z
authors.lastname: Yu
authors.forename: Sangeetha
authors.initials: S
authors.lastname: Selvam
authors.forename: Hanbin
authors.initials: H
authors.lastname: Mao
mesh_terms: D000595:Amino Acid Sequence; D055029:Inverted Repeat Sequences; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D014364:Tryptophan / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011506:Proteins; C539234:Trpzip2 protein; D014364:Tryptophan