The Experts below are selected from a list of 2739 Experts worldwide ranked by ideXlab platform

Martiniano M. Ricardi - One of the best experts on this subject based on the ideXlab platform.

  • Zinc-mediated ASR1 folding.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    A) CD spectrum changes for ASR1 (2 μM) after the addition of increasing amounts of ZnCl2; inset: Mean Residual Molar Ellipticity at 222 nm and % of calculated α-helix as a function of Zn2+ concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 5). B) Elution profile of ASR1 (63 μg) by SEC using an analytical Superdex 75 column: without Zn2+ (full Line) and with 10 μM Zn2+ (dash Line); inset: Molar weight determination by SLS for the protein without Zn2+ addition. C) DLS measurements of 40 μM ASR1 with 0, 5 and 10 μM Zn2+. Frequency histogram of hydrodynamic radius (logarithmic scale) is plotted with the corresponding standard deviation.

  • ASR1 secondary structure in different environments.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    CD spectra of ASR1 (10 μM). A) At different TFE concentrations from 0 (thick Line) to 50%, inset: Mean Residual Molar Ellipticity at 222 and % of calculated α-helix as a function of TFE concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 4) B) At different GdnCl concentrations (0 M in thick Line); inset, differential spectrum between 6 M and 0 M. C) At increasing temperatures (from 5 to 90°C); inset, differential spectrum between 5°C and 90°C. D) At pH 2, 3, 4, 5, 6, 7 and 8; inset, differential spectrum between pH 5 and pH 8. E) At increasing amounts of NaCl; inset, difference spectrum between 1 M and 0 M. F) Without any stabilizing or denaturant agents (full Line) in the presence of crowding agents: 40% of PEG 4000 (dash Line) or 50% glycerol (dotted Line). More noticeable spectral changes are shown in arrowheads in the inset figures.

Diana E. Wetzler - One of the best experts on this subject based on the ideXlab platform.

  • Zinc-mediated ASR1 folding.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    A) CD spectrum changes for ASR1 (2 μM) after the addition of increasing amounts of ZnCl2; inset: Mean Residual Molar Ellipticity at 222 nm and % of calculated α-helix as a function of Zn2+ concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 5). B) Elution profile of ASR1 (63 μg) by SEC using an analytical Superdex 75 column: without Zn2+ (full Line) and with 10 μM Zn2+ (dash Line); inset: Molar weight determination by SLS for the protein without Zn2+ addition. C) DLS measurements of 40 μM ASR1 with 0, 5 and 10 μM Zn2+. Frequency histogram of hydrodynamic radius (logarithmic scale) is plotted with the corresponding standard deviation.

  • ASR1 secondary structure in different environments.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    CD spectra of ASR1 (10 μM). A) At different TFE concentrations from 0 (thick Line) to 50%, inset: Mean Residual Molar Ellipticity at 222 and % of calculated α-helix as a function of TFE concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 4) B) At different GdnCl concentrations (0 M in thick Line); inset, differential spectrum between 6 M and 0 M. C) At increasing temperatures (from 5 to 90°C); inset, differential spectrum between 5°C and 90°C. D) At pH 2, 3, 4, 5, 6, 7 and 8; inset, differential spectrum between pH 5 and pH 8. E) At increasing amounts of NaCl; inset, difference spectrum between 1 M and 0 M. F) Without any stabilizing or denaturant agents (full Line) in the presence of crowding agents: 40% of PEG 4000 (dash Line) or 50% glycerol (dotted Line). More noticeable spectral changes are shown in arrowheads in the inset figures.

Michael Stroscio - One of the best experts on this subject based on the ideXlab platform.

  • Total emission electron scattering rate as a function of the electron energy in the three-layered heterostructure of wurtzite GaN/InGaN/GaN quantum wells.
    2019
    Co-Authors: Ahmed Mohamed, Kihoon Park, Can Bayram, Mitra Dutta, Michael Stroscio
    Abstract:

    The case d = 5 nm is shown for interface in Fig 5A and confined in Fig 5B. The thickness is set to 4nm in Fig 5C and Fig 5D, 3 nm in Fig 5E and Fig 5F and 2 nm in Fig 5G and Fig 5H. Only the phonon-assisted emission for IF (Fig 5A, 5C, 5E and 5G) and confined modes (Fig 5B, 5D, 5F and 5H) is considered. The black Solid Line Corresponds to the total emission rate which is the sum of the IF LO emission, LO absorption and the TO emission rates. For both symmetric and asymmetric emission, the magenta Line Corresponds to LO emission rates, the green Line Corresponds to LO absorption rates, the red Line Corresponds to TO emission rates. The TO emission threshold energies are indicated by blue arrows and are labeled in the graphs as for confined and for IF while the LO emission threshold energies are labeled as for confined and for IF.

Federico Fuchs Wightman - One of the best experts on this subject based on the ideXlab platform.

  • Zinc-mediated ASR1 folding.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    A) CD spectrum changes for ASR1 (2 μM) after the addition of increasing amounts of ZnCl2; inset: Mean Residual Molar Ellipticity at 222 nm and % of calculated α-helix as a function of Zn2+ concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 5). B) Elution profile of ASR1 (63 μg) by SEC using an analytical Superdex 75 column: without Zn2+ (full Line) and with 10 μM Zn2+ (dash Line); inset: Molar weight determination by SLS for the protein without Zn2+ addition. C) DLS measurements of 40 μM ASR1 with 0, 5 and 10 μM Zn2+. Frequency histogram of hydrodynamic radius (logarithmic scale) is plotted with the corresponding standard deviation.

  • ASR1 secondary structure in different environments.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    CD spectra of ASR1 (10 μM). A) At different TFE concentrations from 0 (thick Line) to 50%, inset: Mean Residual Molar Ellipticity at 222 and % of calculated α-helix as a function of TFE concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 4) B) At different GdnCl concentrations (0 M in thick Line); inset, differential spectrum between 6 M and 0 M. C) At increasing temperatures (from 5 to 90°C); inset, differential spectrum between 5°C and 90°C. D) At pH 2, 3, 4, 5, 6, 7 and 8; inset, differential spectrum between pH 5 and pH 8. E) At increasing amounts of NaCl; inset, difference spectrum between 1 M and 0 M. F) Without any stabilizing or denaturant agents (full Line) in the presence of crowding agents: 40% of PEG 4000 (dash Line) or 50% glycerol (dotted Line). More noticeable spectral changes are shown in arrowheads in the inset figures.

Hernan A. Bucci - One of the best experts on this subject based on the ideXlab platform.

  • Zinc-mediated ASR1 folding.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    A) CD spectrum changes for ASR1 (2 μM) after the addition of increasing amounts of ZnCl2; inset: Mean Residual Molar Ellipticity at 222 nm and % of calculated α-helix as a function of Zn2+ concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 5). B) Elution profile of ASR1 (63 μg) by SEC using an analytical Superdex 75 column: without Zn2+ (full Line) and with 10 μM Zn2+ (dash Line); inset: Molar weight determination by SLS for the protein without Zn2+ addition. C) DLS measurements of 40 μM ASR1 with 0, 5 and 10 μM Zn2+. Frequency histogram of hydrodynamic radius (logarithmic scale) is plotted with the corresponding standard deviation.

  • ASR1 secondary structure in different environments.
    2018
    Co-Authors: Diana E. Wetzler, Federico Fuchs Wightman, Hernan A. Bucci, Jimena Rinaldi, Julio J. Caramelo, Norberto D. Iusem, Martiniano M. Ricardi
    Abstract:

    CD spectra of ASR1 (10 μM). A) At different TFE concentrations from 0 (thick Line) to 50%, inset: Mean Residual Molar Ellipticity at 222 and % of calculated α-helix as a function of TFE concentration. The Solid Line Corresponds to the fit of 1:1 binding model (Eq 4) B) At different GdnCl concentrations (0 M in thick Line); inset, differential spectrum between 6 M and 0 M. C) At increasing temperatures (from 5 to 90°C); inset, differential spectrum between 5°C and 90°C. D) At pH 2, 3, 4, 5, 6, 7 and 8; inset, differential spectrum between pH 5 and pH 8. E) At increasing amounts of NaCl; inset, difference spectrum between 1 M and 0 M. F) Without any stabilizing or denaturant agents (full Line) in the presence of crowding agents: 40% of PEG 4000 (dash Line) or 50% glycerol (dotted Line). More noticeable spectral changes are shown in arrowheads in the inset figures.