title: Identification of the folding inhibitors of hen-egg lysozyme: gathering the right tools.
abstract: The unfolded state of proteins displays a surprisingly rich amount of local native structure, which appears to be critical for driving the protein to its native state. Peptides with the same sequence of the corresponding structured segments can be used to interfere with the correct folding of the protein. Using model simulations, we investigate the folding of hen-egg lysozyme, identifying its key segments. Activity assays, NMR and circular dichroism experiments are used to screen the peptides which are able to inhibit the folding of lysozyme. Few peptides, corresponding to the segments of the protein which are structured in the unfolded state, are identified to have significant inhibitory effects.
authors.affiliation: Dipartimento di Fisica, Universitá di Milano, via Celoria 16, Milan, Italy.
authors.forename: Martina
authors.initials: M
authors.lastname: Caldarini
authors.forename: Ludovico
authors.initials: L
authors.lastname: Sutto
authors.forename: Carlo
authors.initials: C
authors.lastname: Camilloni
authors.forename: Francesca
authors.initials: F
authors.lastname: Vasile
authors.forename: Ricardo A
authors.initials: RA
authors.lastname: Broglia
authors.forename: Guido
authors.initials: G
authors.lastname: Tiana