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Literature DB >> 2172017

Secondary structure of a mitochondrial signal peptide in lipid bilayer membranes.

Abstract

The secondary structure of the synthetic signal peptide of cytochrome c oxidase subunit IV (coxIV-25) has been measured by circular dichroism spectroscopy in different lipid environments. CoxIV-25 is polymorphic in membranes. It forms an amphiphilic alpha-helix both in negatively charged lipid bilayers (up to 49% helix) and in detergent micelles (up to 42% helix). In association with bilayers of the zwitterionic lipid phosphatidylcholine, coxIV-25 takes an aperiodic, unidentified structure. CoxIV-25 is also partially alpha-helical in bilayers of cardiolipin, mitochondrial lipid extracts and mixtures of synthetic phosphatidylcholine and phosphatidylglycerol.

Entities: Chemical Gene

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Year: 1990 PMID： 2172017 DOI： 10.1016/0014-5793(90)80441-k

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

6 in total

6. Truncated presequences of mitochondrial F1-ATPase beta subunit from Nicotiana plumbaginifolia transport CAT and GUS proteins into mitochondria of transgenic tobacco.

Authors: F Chaumont; M de C Silva Filho; D Thomas; S Leterme; M Boutry
Journal: Plant Mol Biol Date: 1994-02 Impact factor: 4.076

6 in total

Secondary structure of a mitochondrial signal peptide in lipid bilayer membranes.

1. Binding of a synthetic targeting peptide to a mitochondrial channel protein.

2. A spectroscopic study of the mitochondrial transit peptide of rat malate dehydrogenase.

3. Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide.

4. Influence of the membrane dipole potential on peptide binding to lipid bilayers.

5. sCD44 internalization in human trabecular meshwork cells.

6. Truncated presequences of mitochondrial F1-ATPase beta subunit from Nicotiana plumbaginifolia transport CAT and GUS proteins into mitochondria of transgenic tobacco.