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Data in support of intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures.

Odahara T, Odahara K - Data Brief (2016)

Bottom Line: The data provide information in support of the research article, "Intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures" [1].The data regarding variation of absorption spectra is used as an indicator of the duration of Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2 in the native state in the presence of NaCl/polyethylene glycol (PEG) mixture.The data about minimum concentrations of salt and PEG whose aqueous phases are mutually separated presents information on additional influence of Tris buffer and N-octyl-β-d-glucoside on the salt-PEG phase separation.

View Article: PubMed Central - PubMed

Affiliation: National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central-6, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

ABSTRACT
The data provide information in support of the research article, "Intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures" [1]. The data regarding variation of absorption spectra is used as an indicator of the duration of Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2 in the native state in the presence of NaCl/polyethylene glycol (PEG) mixture. The data about minimum concentrations of salt and PEG whose aqueous phases are mutually separated presents information on additional influence of Tris buffer and N-octyl-β-d-glucoside on the salt-PEG phase separation.

No MeSH data available.


Related in: MedlinePlus

Absorption spectra of integral membrane proteins from photosynthetic bacteria stored at 20 °C in darkness in the presence of NaCl/PEG mixture. The examined proteins were Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2. The spectra of each protein were measured for the purified sample (blue line) and the supernatants within 1 h (black dotted line) and in 14–35 days (red line) after the mixture addition. The longer duration was 14, 15, 21 35 and 28 days for Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2, respectively. The spectra were measured for protein solutions diluted by detergent-containing buffer solution (25 mM Tris–HCl and 300 mM NaCl; pH 8.0) of which the maximum absorbance was below 2. The spectra exhibited were scaled so as to fit their base lines to one another. The PEG concentration in the original supernatant was 62.5 mg/mL for Rp. viridis PRU/LM, 70 mg/mL for Rp. viridis RC/LM, 160 mg/mL for Rb. sphaeroides RC/LDAO, 150 mg/mL for Rb. sphaeroides LH2/LDAO, and 150 mg/mL for Rb. capsulatus LH2/LDAO. The concentration of LM and LDAO was 1 mg/mL.
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f0005: Absorption spectra of integral membrane proteins from photosynthetic bacteria stored at 20 °C in darkness in the presence of NaCl/PEG mixture. The examined proteins were Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2. The spectra of each protein were measured for the purified sample (blue line) and the supernatants within 1 h (black dotted line) and in 14–35 days (red line) after the mixture addition. The longer duration was 14, 15, 21 35 and 28 days for Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2, respectively. The spectra were measured for protein solutions diluted by detergent-containing buffer solution (25 mM Tris–HCl and 300 mM NaCl; pH 8.0) of which the maximum absorbance was below 2. The spectra exhibited were scaled so as to fit their base lines to one another. The PEG concentration in the original supernatant was 62.5 mg/mL for Rp. viridis PRU/LM, 70 mg/mL for Rp. viridis RC/LM, 160 mg/mL for Rb. sphaeroides RC/LDAO, 150 mg/mL for Rb. sphaeroides LH2/LDAO, and 150 mg/mL for Rb. capsulatus LH2/LDAO. The concentration of LM and LDAO was 1 mg/mL.

Mentions: Fig. 1 shows representatives of the spectra measured at various time points after the addition of NaCl/PEG mixture. At one hour or shorter time points after the mixture addition, no variations in the spectra were observed for all the proteins. After several to 30 days, however, four proteins excluding Rb. sphaeroides RC exhibited variation in their absorption spectra that reflected variation of the intramolecular cofactors and the peptides supporting them. With Rp. viridis PRU, the absorption band with a maximum at 1006 nm, arising from bacteriochlorophyll in the LH1 subunits, decreased and a new peak appeared at 687 nm. In the spectra of Rp. viridis RC, the absorption band with a maximum at 830 nm, arising from special pair of bacteriochlorophyll, disappeared. With Rb. sphaeroides LH2 and Rb. capsulatus LH2, the two absorption peaks at 800 nm and 850 nm decreased and a small peak appeared at 690 nm.


Data in support of intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures.

Odahara T, Odahara K - Data Brief (2016)

Absorption spectra of integral membrane proteins from photosynthetic bacteria stored at 20 °C in darkness in the presence of NaCl/PEG mixture. The examined proteins were Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2. The spectra of each protein were measured for the purified sample (blue line) and the supernatants within 1 h (black dotted line) and in 14–35 days (red line) after the mixture addition. The longer duration was 14, 15, 21 35 and 28 days for Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2, respectively. The spectra were measured for protein solutions diluted by detergent-containing buffer solution (25 mM Tris–HCl and 300 mM NaCl; pH 8.0) of which the maximum absorbance was below 2. The spectra exhibited were scaled so as to fit their base lines to one another. The PEG concentration in the original supernatant was 62.5 mg/mL for Rp. viridis PRU/LM, 70 mg/mL for Rp. viridis RC/LM, 160 mg/mL for Rb. sphaeroides RC/LDAO, 150 mg/mL for Rb. sphaeroides LH2/LDAO, and 150 mg/mL for Rb. capsulatus LH2/LDAO. The concentration of LM and LDAO was 1 mg/mL.
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f0005: Absorption spectra of integral membrane proteins from photosynthetic bacteria stored at 20 °C in darkness in the presence of NaCl/PEG mixture. The examined proteins were Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2. The spectra of each protein were measured for the purified sample (blue line) and the supernatants within 1 h (black dotted line) and in 14–35 days (red line) after the mixture addition. The longer duration was 14, 15, 21 35 and 28 days for Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2, respectively. The spectra were measured for protein solutions diluted by detergent-containing buffer solution (25 mM Tris–HCl and 300 mM NaCl; pH 8.0) of which the maximum absorbance was below 2. The spectra exhibited were scaled so as to fit their base lines to one another. The PEG concentration in the original supernatant was 62.5 mg/mL for Rp. viridis PRU/LM, 70 mg/mL for Rp. viridis RC/LM, 160 mg/mL for Rb. sphaeroides RC/LDAO, 150 mg/mL for Rb. sphaeroides LH2/LDAO, and 150 mg/mL for Rb. capsulatus LH2/LDAO. The concentration of LM and LDAO was 1 mg/mL.
Mentions: Fig. 1 shows representatives of the spectra measured at various time points after the addition of NaCl/PEG mixture. At one hour or shorter time points after the mixture addition, no variations in the spectra were observed for all the proteins. After several to 30 days, however, four proteins excluding Rb. sphaeroides RC exhibited variation in their absorption spectra that reflected variation of the intramolecular cofactors and the peptides supporting them. With Rp. viridis PRU, the absorption band with a maximum at 1006 nm, arising from bacteriochlorophyll in the LH1 subunits, decreased and a new peak appeared at 687 nm. In the spectra of Rp. viridis RC, the absorption band with a maximum at 830 nm, arising from special pair of bacteriochlorophyll, disappeared. With Rb. sphaeroides LH2 and Rb. capsulatus LH2, the two absorption peaks at 800 nm and 850 nm decreased and a small peak appeared at 690 nm.

Bottom Line: The data provide information in support of the research article, "Intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures" [1].The data regarding variation of absorption spectra is used as an indicator of the duration of Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2 in the native state in the presence of NaCl/polyethylene glycol (PEG) mixture.The data about minimum concentrations of salt and PEG whose aqueous phases are mutually separated presents information on additional influence of Tris buffer and N-octyl-β-d-glucoside on the salt-PEG phase separation.

View Article: PubMed Central - PubMed

Affiliation: National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central-6, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

ABSTRACT
The data provide information in support of the research article, "Intermolecular interactions at early stage of protein/detergent particle association induced by salt/polyethylene glycol mixtures" [1]. The data regarding variation of absorption spectra is used as an indicator of the duration of Rp. viridis PRU and RC, Rb. sphaeroides RC and LH2, and Rb. capsulatus LH2 in the native state in the presence of NaCl/polyethylene glycol (PEG) mixture. The data about minimum concentrations of salt and PEG whose aqueous phases are mutually separated presents information on additional influence of Tris buffer and N-octyl-β-d-glucoside on the salt-PEG phase separation.

No MeSH data available.


Related in: MedlinePlus