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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Biochemistry

Proton NMR conformational study of an annexin I fragment: influence of a phospholipidic micellar environment

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 20 Jul 1993

Macquaire F, Baleux F, Huynh-Dinh T, Rouge D, Neumann JM, Sanson A

Link to Pubmed [PMID] – 8393708

Biochemistry 1993 Jul;32(28):7244-54

A 32 residue peptide, Ac-AQWDADELRAAMKGLGTDEDTLIELASRTNK, spanning the first helix-loop-helix motif of the second repeat of human annexin I, was synthesized and studied by standard 2D proton NMR and molecular modeling. The peptide was solubilized either in aqueous solution, in TFE-H2O mixtures or in aqueous phospholipidic micellar solution. In pure aqueous solution, elements of helix secondary structure were observed. Addition of TFE led to a dramatic cooperative effect on the secondary structure with a very low transition midpoint indicative of the strong tendency of the peptide to form alpha helices. Only in the aqueous micellar solution was the full helix-loop-helix motif obtained, showing again the potency of a membrane-like micellar environment to initiate peptide secondary structures and even elements of tertiary structure. There were sufficient NMR data to perform molecular modeling of the structure of the annexin fragment solubilized in the presence of micelles. However, this structure showed a relatively high degree of flexibility, especially around the T17-D18 hinge at the end of the loop.

http://www.ncbi.nlm.nih.gov/pubmed/8393708