Related ArticlesNMR structures of a mitochondrial transit peptide from the green alga Chlamydomonas reinhardtii.
FEBS Lett. 1996 Aug 5;391(1-2):203-8
Authors: Lancelin JM, Gans P, Bouchayer E, Bally I, Arlaud GJ, Jacquot JP
The 26-amino-acid pre-sequence of the ATP synthase beta subunit that directs the protein from the cytosol to mitochondria in the unicellular green alga Chlamydomonas reinhardtii has been synthesised and analysed using NMR spectroscopy/circular dichroism and compared to a chloroplast transit peptide from the same organism. The results demonstrate that the peptide, though mainly unstructured in water, undergoes a strong conformational change in a 36% water/64% 2,2,2-trifluoroethanol mixture. In this solvent condition, an alpha-helix was characterised by NMR from residue 2 to 26. Structure calculations under NMR restraints lead to a population of models of which 60% are kinked at position 9-10. Structural analysis indicates two hydrophobic sectors on the models with a discontinuity at the 9-10 kink level. The structures suggest a different interaction mode with the mitochondrial membrane compared to the chloroplast transit peptide.
Postdoctoral position in electrochemistry/ organic synthesis | Bowling Green State University
Postdoctoral position in electrochemistry/ organic synthesis | Bowling Green State University
US - Bowling Green, OH, PhD in organic electrochemistry is favored. The candidate is expected to perform multistep syntheses with product characterization using NMR, MS and other techniques. In addition, the candidate is exp
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NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
Biophys J. 2010 Oct 20;99(8):2507-15
Authors: Georgescu J, Munhoz VH, Bechinger B
The LAH4 family of histidine-rich peptides exhibits potent antimicrobial and DNA transfection activities, both of which require interactions...
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[NMR paper] The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a compa
The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a comparison with the structure of microcystin-LR.
Related Articles The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a comparison with the structure of microcystin-LR.
Eur J Biochem. 1998 Dec 1;258(2):301-12
Authors: Trogen GB, Edlund U, Larsson G, Sethson I
The microcystin-RR structures are compared with the structures of microcystin-LR in solution as well as in the crystal structure of the complex with protein phosphatase. The gross...
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[NMR paper] The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii
The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Related Articles The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Eur J Biochem. 1998 Jul 1;255(1):185-95
Authors: Krimm I, Lemaire S, Ruelland E, Miginiac-Maslow M, Jaquot JP, Hirasawa M, Knaff DB, Lancelin JM
The role of the invariant Trp...
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[NMR paper] Trans-membrane peptide and protein structures in fluid membranes via NMR.
Trans-membrane peptide and protein structures in fluid membranes via NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Trans-membrane peptide and protein structures in fluid membranes via NMR.
Biophys J. 1995 Nov;69(5):1631-2
Authors: Bloom M
[NMR paper] 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
Related Articles 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
Biochemistry. 1990 Oct 23;29(42):9872-8
Authors: Karslake C, Piotto ME, Pak YK, Weiner H, Gorenstein DG
The 19 amino acid signal peptide of rat liver aldehyde dehydrogenase, possessing a lysine substitution for an arginine and containing 3 extra amino acid residues at the C terminus, was studied by two-dimensional NMR in a dodecylphosphocholine micelle. In this...
NMR structures of a mitochondrial transit peptide from the green alga Chlamydomonas r
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