title: Role of tryptophanyl residues in driving myoglobin folding.
abstract: Mammalian myoglobins contain two tryptophanyl residues at the invariant positions 7 (A-5) and 14 (A-12) in the N-terminal region (A helix) of the protein molecule. The simultaneous substitution of both tryptophanyl residues causes an incorrect folding with subsequent loss of heme binding. The introduction of a indolic residue in different molecular regions, i.e. G, E, and C helix resulted in a not correctly folded protein, suggesting that the tryptophanyl residues are strong structural determinants.
authors.affiliation: Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli.
authors.forename: I
authors.initials: I
authors.lastname: Sirangelo
authors.forename: M
authors.initials: M
authors.lastname: Casillo
authors.forename: C
authors.initials: C
authors.lastname: Malmo
authors.forename: G
authors.initials: G
authors.lastname: Irace
mesh_terms: D000818:Animals; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014364:Tryptophan / Q000737:chemistry* / Q000235:genetics; D014907:Whales
chemical_list: D009211:Myoglobin; D014364:Tryptophan