1fct | pdb_00001fct
NMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM CHLAMYDOMONAS REINHARDTII PROMOTED BY TRIFLUOROETHANOL IN AQUEOUS SOLUTION
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Overview
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 alpha-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 CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a, hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced, alpha-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.
About this Structure
1FCT is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution., Lancelin JM, Bally I, Arlaud GJ, Blackledge M, Gans P, Stein M, Jacquot JP, FEBS Lett. 1994 May 2;343(3):261-6. PMID:8174712
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