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What is the basic structure of α-keratin?
Two α-helical chains twist around each other to form a left-handed coiled-coil dimer.
What is the pitch of α-keratin compared with a normal α-helix?
α-Keratin: 5.1 Å; normal α-helix: 5.4 Å.
What stabilizes α-keratin?
Disulfide bonds between cysteine residues.
How do hard and soft α-keratin differ?
Hard keratin has high sulfur content and is less pliable; soft keratin has low sulfur content and is more pliable.
What is the assembly sequence of α-keratin?
Coiled-coil dimers → protofilaments → protofibrils → microfibrils → macrofibrils.
Where is keratin found?
Epidermis, hair, nails, horns, and feathers.