Online Table I parameters of the fluorescence emission spectra of mTM4 and mTM10 in various media








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titreOnline Table I parameters of the fluorescence emission spectra of mTM4 and mTM10 in various media
date de publication06.01.2017
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Online Table I Parameters of the fluorescence emission spectra of mTM4 and mTM10 in various media

Peptide

Medium

λmax (nm)

mTM4

Pure TFE

340

mTM4

TFE/H2O (50/50, v/v)

342.5

mTM4

DPC micelles

320

mTM4

DDM micelles

318.5

mTM4

Buffer

328.5

mTM10

Pure TFE

307.5

mTM10

TFE/H2O (50/50, v/v)

339

mTM10

DPC micelles

331

mTM10

DDM micelles

327

mTM10

Buffer

329.5

Standard conditions: λex=280 nm, slits 1.25 mm at excitation and emission (λmax for NATA in water was 352 nm in these conditions); 10 µM peptide; buffer: 10 mM potassium phosphate pH 7.5. Detergent was 4 mM in buffer. T=20°C

Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics

European Biophysics Journal

Béatrice de Forestaa,b Michel Vincent, Manuel Garrigos and Jacques Gallayc,d

aCEA, iBiTecS, Service de Bioénergétique Biologie Structurale et Mécanismes, F-91191, Gif-sur-Yvette, France; bCNRS, URA 2096, F-91191, Gif-sur-Yvette, France; cUniversité Paris-Sud 11, UMR 8619, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Bât. 430, Orsay, France; dCNRS, UMR 8619, Orsay, France

Corresponding authors.

B. de Foresta: beatrice.de-foresta@cea.fr

J. Gallay: jacques.gallay@u-psud.fr

Online Table II Characteristics for predicted transmembrane fragments of hMRP1

Domain

Peptide

name

Sequence

Charge

ΔG Unstructured

(kcal/mol)

MSD0

TM1

CF-QNTVLVWVPCFYLWACFPFYF-LY

0

-14.7




TM2

TK-TALGFLLWIVCWADLFYSFWE-RS

++,--

-9.21




TM3

RGY-FLAPVFLVSPTLLGITTLLAT-F

+

-7.02




TM4

VQ-SSGIMLTFWLVALVCALAILR-SK

++

-5.78




TM5

RD-ITFYVYFSLLLIQLVLSCFSD-RS

++,--

-6.02

MSD1

TM6

KV-LYKTFGPYFLMSFFFKAIHDL-MM

4+,-

-6.63




TM7

(W)QG-YFYTVLLFVTACLQTLVLHQY-FH

++

-7.33




TM8

TY-INMIWSAPLQVILALYLLWLN-LG

0

-10.21




TM9

GP-SVLAGVAVMVLMVPVNAVMAM-KT

+

-0.82




TM10

SA-VGTFTWVCTPFLVALCTFAVY-VT

0

-8.18




TM11

FN-ILRFPLNILPMVISSIVQASV-SL

+

-4.49

MSD2

TM12

(WD)YM-KAIGLFISFLSIFLFMCNHVS-AL

++

-8.7




TM13

IS-QGIAVFGYSMAVSIGGILASR-CL

+

-4.85




TM14

PE-VIKMFMGSLFNVIGACIVILL-AT

+,-

-3.71




TM15

LA-TPIAAIIIPPLGLIYFFVQRF-YV

+

-7.06




TM16

ANRWLAVRL-ECVGNCIVLFAALFAV(ISRHS-LS)

++,-

-4.07




TM17

(LS-)AGVGLSVSYSLQVTTTYLNWL-VRMS

+

-6.23

The sequences were the 21 amino-acid sequences predicted for human MRP1 (from Swissprot-Uniprot-hMRP, code P33527), to which we added the N-terminal and C-terminal amino acids from the same sequence, unless otherwise stated. TM16 and 17 were slightly more extended on the cytoplasmic side. In parentheses: Trp close to TM or Uniprot-predicted TM sequences.

Hydropathy color code: Hydrophobic Polar Basic Acidic.

Free energy: From MPEX 3.0, N-T acetylated, C-T CONH2, partitioning from water to bilayer, TM: n=25

Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics

European Biophysics Journal

Béatrice de Forestaa,b Michel Vincent, Manuel Garrigos and Jacques Gallayc,d

aCEA, iBiTecS, Service de Bioénergétique Biologie Structurale et Mécanismes, F-91191, Gif-sur-Yvette, France; bCNRS, URA 2096, F-91191, Gif-sur-Yvette, France; cUniversité Paris-Sud 11, UMR 8619, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Bât. 430, Orsay, France; dCNRS, UMR 8619, Orsay, France

Corresponding authors.

B. de Foresta: beatrice.de-foresta@cea.fr

J. Gallay: jacques.gallay@u-psud.fr



Online Figure I Kinetics of the titration of mTM4 with DPC and DDM

We added 10 µM mTM4 to 10 mM potassium phosphate buffer, pH 7.5, at 20°C (first arrow). Aliquots of DPC (black trace) or DDM (blue trace) (series of black and blue arrows respectively) were then added sequentially, with continuous stirring, at constant intervals (~50 s). For DPC (cmc=1.1 mM), final concentrations in the cuvette were 0.5, 1, 2, 4 and 6 mM. For DDM (cmc=0.17 mM), final concentrations were 0.1, 0.2, 1, 2, 3 and 6 mM. Fluorescence intensity was recorded continuously with ex set at 280 nm and λem at 320 nm. Slit widths were 1.25 mm (bandwidths ~5 nm) for both excitation and emission

Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics

European Biophysics Journal

Béatrice de Forestaa,b Michel Vincent, Manuel Garrigos and Jacques Gallayc,d

aCEA, iBiTecS, Service de Bioénergétique Biologie Structurale et Mécanismes, F-91191, Gif-sur-Yvette, France; bCNRS, URA 2096, F-91191, Gif-sur-Yvette, France; cUniversité Paris-Sud 11, UMR 8619, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Bât. 430, Orsay, France; dCNRS, UMR 8619, Orsay, France

Corresponding authors.

B. de Foresta: beatrice.de-foresta@cea.fr

J. Gallay: jacques.gallay@u-psud.fr

Online Figure II Fluorescence emission spectra of the hMRP1 fragments in various media

A: Emission spectra for 10 µM mTM4 in TFE/water (50/50, v/v) (long dashed lines) or TFE (short dashed line). ex was set at 280 nm. Slit widths were 1.25 mm (bandwidths ~5 nm) for both excitation and emission. Spectra were recorded after a short period of equilibration (2-3 min) and the readings for background spectra (same solvent or detergent in buffer) were subtracted.

B: Emission spectra for 10 µm mTM10. Same symbols as in panel A.

In both panels, the emission spectrum of 10 µM NATA in pure water is indicated as a reference (green line)

Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics

European Biophysics Journal

Béatrice de Forestaa,b Michel Vincent, Manuel Garrigos and Jacques Gallayc,d

aCEA, iBiTecS, Service de Bioénergétique Biologie Structurale et Mécanismes, F-91191, Gif-sur-Yvette, France; bCNRS, URA 2096, F-91191, Gif-sur-Yvette, France; cUniversité Paris-Sud 11, UMR 8619, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Bât. 430, Orsay, France; dCNRS, UMR 8619, Orsay, France

Corresponding authors.

B. de Foresta: beatrice.de-foresta@cea.fr

J. Gallay: jacques.gallay@u-psud.fr

Online Figure III Fluorescence emission spectra of mTM4 in mixed micelles of BrDDM/DDM (panel A) or BrUM/DDM (panel B)

A: Emission spectra for 5 µM mTM4 in 10 mM potassium phosphate buffer, pH 7.5, supplemented with various mixtures of BrDDM and DDM, at a final total detergent concentration of 4 mM, at 20°C. X, the molar fraction of BrDDM was 0, 0.1, 0.2, 0.4, 0.6 or 1 (from upper to lower spectra). ex was set at 280 nm. Slit widths were 1.25 mm (bandwidths ~5 nm) for both excitation and emission. Spectra were recorded after a short period of equilibration (~3 min) and the readings for background spectra (detergent in buffer) were subtracted.

B: Similar experiment to that in panel A, with BrUM as the brominated detergent

Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics

European Biophysics Journal

Béatrice de Forestaa,b Michel Vincent, Manuel Garrigos and Jacques Gallayc,d

aCEA, iBiTecS, Service de Bioénergétique Biologie Structurale et Mécanismes, F-91191, Gif-sur-Yvette, France; bCNRS, URA 2096, F-91191, Gif-sur-Yvette, France; cUniversité Paris-Sud 11, UMR 8619, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Bât. 430, Orsay, France; dCNRS, UMR 8619, Orsay, France

Corresponding authors.

B. de Foresta: beatrice.de-foresta@cea.fr

J. Gallay: jacques.gallay@u-psud.fr

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