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The structural flexibility of the preferredoxin transit peptide
Author(s) -
Wienk Hans L.J.,
Czisch Michael,
de Kruijff Ben
Publication year - 1999
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(99)00653-5
Subject(s) - circular dichroism , polyproline helix , peptide , transit peptide , chemistry , helix (gastropod) , stereochemistry , protein secondary structure , amino acid , nuclear magnetic resonance spectroscopy , crystallography , chloroplast , biochemistry , biology , ecology , plastid , snail , gene
In order to obtain insight into the structural flexibility of chloroplast targeting sequences, the Silene pratensis preferredoxin transit peptide was studied by circular dichroism and nuclear magnetic resonance spectroscopy. In water, the peptide is unstructured, with a minor propensity towards helix formation from Val‐9 to Ser‐12 and from Gly‐30 to Ser‐40. In 50% (v/v) trifluoroethanol, structurally independent N‐ and C‐terminal helices are stabilized. The N‐terminal helix appears to be amphipathic, with hydrophobic and hydroxylated amino acids on opposite sides. The C‐terminal helix comprises amino acids Met‐29–Gly‐50 and is destabilized at Gly‐39. No ordered tertiary structure was observed. The results are discussed in terms of protein import into chloroplasts, in which the possible interactions between the transit peptide and lipids are emphasized.