Immunoglobulin domain
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The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, consisting of about 125 amino acids.
Structure of an antigen binding fragment of an antibody.
Titin
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Titin is a protein that in humans is encoded by the TTN gene. Titin is a protein, over 1 µm in length, that functions as a molecular spring that is responsible for the passive elasticity of muscle. It comprises 244 individually folded protein domains connected by unstructured peptide sequences. These domains unfold when the protein is stretched and refold when the tension is removed.
Titin Ig domains. a) Schematic of part of a sarcomere b) Structure of Ig domains c) Topology of Ig domains.
Reconstruction of the thin (green) and thick filament from mammalian cardiac tissue. Myosin is in blue, MyBP-C is in yellow, and titin is in two shades of red (dark red for titin-alpha and light red for titin-beta).