University of Hertfordshire

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Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids. / Berkhout, Theo; Rietveld, A.; de Kruijff, Ben.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 897, No. 1, 12.02.1987, p. 1-4.

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@article{adacb0d689bc42b4badfe390bdc5fcc1,
title = "Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids",
abstract = "The fluorescence of the single tryptophan residue at position 59 in apocytochrome c, the biosynthetic precursor of the inner mitochondrial membrane protein cytochrome c, was studied in small unilamellar vesicles composed of phosphatidylserine (PS) and phosphatidylcholine (PC) with or without specifically Br-labelled acyl chains at the sn-2 position. The protein has a very high affinity for PS-containing vesicles (dissociation constant Kd less than 1 microM). From the relative quenching efficiency by the brominated phospholipids, it could be concluded that the protein specifically associates with the PS component in mixed vesicles and that maximal quenching occurred with phospholipids in which the bromine was present at the 6,7-position of the 2-acyl chain suggesting that (part of) the bound protein penetrates 7-8 A deep into the hydrophobic core of the bilayer.",
keywords = "Apoproteins, Bromine, Cytochrome c Group, Cytochromes c, Membranes, Artificial, Phosphatidylcholines, Phosphatidylserines, Protein Conformation, Spectrometry, Fluorescence, Tryptophan",
author = "Theo Berkhout and A. Rietveld and {de Kruijff}, Ben",
year = "1987",
month = feb,
day = "12",
doi = "10.1016/0005-2736(87)90308-7",
language = "English",
volume = "897",
pages = "1--4",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids

AU - Berkhout, Theo

AU - Rietveld, A.

AU - de Kruijff, Ben

PY - 1987/2/12

Y1 - 1987/2/12

N2 - The fluorescence of the single tryptophan residue at position 59 in apocytochrome c, the biosynthetic precursor of the inner mitochondrial membrane protein cytochrome c, was studied in small unilamellar vesicles composed of phosphatidylserine (PS) and phosphatidylcholine (PC) with or without specifically Br-labelled acyl chains at the sn-2 position. The protein has a very high affinity for PS-containing vesicles (dissociation constant Kd less than 1 microM). From the relative quenching efficiency by the brominated phospholipids, it could be concluded that the protein specifically associates with the PS component in mixed vesicles and that maximal quenching occurred with phospholipids in which the bromine was present at the 6,7-position of the 2-acyl chain suggesting that (part of) the bound protein penetrates 7-8 A deep into the hydrophobic core of the bilayer.

AB - The fluorescence of the single tryptophan residue at position 59 in apocytochrome c, the biosynthetic precursor of the inner mitochondrial membrane protein cytochrome c, was studied in small unilamellar vesicles composed of phosphatidylserine (PS) and phosphatidylcholine (PC) with or without specifically Br-labelled acyl chains at the sn-2 position. The protein has a very high affinity for PS-containing vesicles (dissociation constant Kd less than 1 microM). From the relative quenching efficiency by the brominated phospholipids, it could be concluded that the protein specifically associates with the PS component in mixed vesicles and that maximal quenching occurred with phospholipids in which the bromine was present at the 6,7-position of the 2-acyl chain suggesting that (part of) the bound protein penetrates 7-8 A deep into the hydrophobic core of the bilayer.

KW - Apoproteins

KW - Bromine

KW - Cytochrome c Group

KW - Cytochromes c

KW - Membranes, Artificial

KW - Phosphatidylcholines

KW - Phosphatidylserines

KW - Protein Conformation

KW - Spectrometry, Fluorescence

KW - Tryptophan

U2 - 10.1016/0005-2736(87)90308-7

DO - 10.1016/0005-2736(87)90308-7

M3 - Article

C2 - 3026475

VL - 897

SP - 1

EP - 4

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 1

ER -