Role of tryptophanyl residues in driving myoglobin folding.
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.
Sirangelo
I
I
Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli.
Casillo
M
M
Malmo
C
C
Irace
G
G
D000818:Animals; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014364:Tryptophan / Q000737:chemistry* / Q000235:genetics; D014907:Whales
D009211:Myoglobin; D014364:Tryptophan