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NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution
Author(s) -
Lancelin Jean-Marc,
Bally Isabelle,
J. Arlaud Gérard,
Blackledge Martin,
Gans Pierre,
Stein Mariana,
Jacquot Jean-Pierre
Publication year - 1994
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 - 10.1016/0014-5793(94)80568-7
Subject(s) - chlamydomonas reinhardtii , ferredoxin , chlamydomonas , aqueous solution , chemistry , peptide , biochemistry , enzyme , organic chemistry , gene , mutant
The 32‐amino acid transit peptide of the unicellular green alga Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by NMR spectroscopy and circular dichroism. The results show that while the peptide is unstructured in water, it undergoes an α‐helix formation from residue 3 to 13 in a 30:70 molar‐ratio mixture of 2,2,2‐trifluoroethanol. The remainder of the peptide is still unstructured in CF 3 CD 2 OD/H 2 O mixtures, but is distributed on a side opposite to a hydrophobic ridge formed by Met 5 , Phe 9 and Val 13 on the induced a‐helix. The NMR structures driven by 2,2,2‐trifluoroethanol in aqueous solution, are discussed in terms of potent interactions with the chloroplast envelope and its translocation molecular machinery.