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Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis
Author(s) -
Deng Gejing,
Andrews David W,
Laursen Richard A
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01466-4
Subject(s) - antifreeze protein , peptide sequence , glutamine , circular dichroism , amino acid , antifreeze , biology , biochemistry , sequence (biology) , sequence analysis , helix bundle , helix (gastropod) , chemistry , protein structure , gene , zoology , organic chemistry , gastropoda
A new type of fish antifreeze protein, designated here type IV, has been isolated from the longhorn sculpin, Myoxocephalus octodecimspinosis . Sequence analysis of the protein (LS‐12) reveals that it contains 108 amino acids, is blocked at the N‐terminus by a pyroglutamyl group and has a high (17%) content of glutamine; it is thus completely unrelated to the earlier described types I, II and III fish antifreeze proteins. Circular dichroism spectra and conformational analysis based on the sequence data indicate that LS‐12 has a high helix content and probably folds as a four‐helix bundle. LS‐12 shows sequence similarity to certain plasma apolipoproteins known to have helix bundle structures, suggesting the possibility that LS‐12 may have arisen by recruitment and mutation of a plasma apolipoprotein.