The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Vepatu Shankar - One of the best experts on this subject based on the ideXlab platform.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:Abstract RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37°C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45°C. Compared to the native enzyme at 37°C, the Km and Vmax of RNase Rs at 45°C and in the presence of 2 M urea at 37°C showed an increase while kcat/Km decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37°C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37 degrees C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45 degrees C. Compared to the native enzyme at 37 degrees C, the K(m) and V(max) of RNase Rs at 45 degrees C and in the presence of 2 M urea at 37 degrees C showed an increase while k(cat)/K(m) decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37 degrees C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
Rajashree A Deshpande - One of the best experts on this subject based on the ideXlab platform.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:Abstract RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37°C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45°C. Compared to the native enzyme at 37°C, the Km and Vmax of RNase Rs at 45°C and in the presence of 2 M urea at 37°C showed an increase while kcat/Km decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37°C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37 degrees C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45 degrees C. Compared to the native enzyme at 37 degrees C, the K(m) and V(max) of RNase Rs at 45 degrees C and in the presence of 2 M urea at 37 degrees C showed an increase while k(cat)/K(m) decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37 degrees C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
Beatrice Sala - One of the best experts on this subject based on the ideXlab platform.
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Optimum Temperature range for the proton dynamics in h doped bazro 3 yb dense ceramics a neutron scattering study
Journal of Materials Research, 2012Co-Authors: Aneta Slodczyk, Philippe Colomban, D Lamago, G Andre, Oumaya Zaafrani, Olivier Lacroix, Abdelkader Sirat, Frederic Grasset, Beatrice SalaAbstract:The proton conducting perovskite MZr1−xLnxO3−δHz ceramics are promising electrolytic membranes for fuel cell and water steam electrolyser applications. Simultaneous elastic/quasielastic and diffraction neutron studies were performed in a wide Temperature range (25–1150 °C) on protonated Yb-modified BaZrO3 ceramics: dense (97% of theoretical density) and ultradense (99%) using the triple axis spectrometers. The results allowed us to determine: (i) the real content of bulk protonic species ∼1–5 10−3 mol/mol, (ii) the structural modifications caused by the proton doping, and (iii) the bulk proton dynamics. The quasielastic neutron scattering (QNS) results are discussed in the light of neutron diffraction, conductivity, Raman, thermogravimetric, and thermal expansion measurements. The highest bulk proton motion appears in the Temperature range where the structural modifications and the energy activation changes are detected. This allows defining the Optimum Temperature range for the proton dynamics between 400 and 560 °C.
Ameeta Ravi Kumar - One of the best experts on this subject based on the ideXlab platform.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:Abstract RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37°C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45°C. Compared to the native enzyme at 37°C, the Km and Vmax of RNase Rs at 45°C and in the presence of 2 M urea at 37°C showed an increase while kcat/Km decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37°C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37 degrees C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45 degrees C. Compared to the native enzyme at 37 degrees C, the K(m) and V(max) of RNase Rs at 45 degrees C and in the presence of 2 M urea at 37 degrees C showed an increase while k(cat)/K(m) decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37 degrees C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
Islam M Khan - One of the best experts on this subject based on the ideXlab platform.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:Abstract RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37°C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45°C. Compared to the native enzyme at 37°C, the Km and Vmax of RNase Rs at 45°C and in the presence of 2 M urea at 37°C showed an increase while kcat/Km decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37°C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
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ribonuclease rs from rhizopus stolonifer lowering of Optimum Temperature in the presence of urea
Biochimica et Biophysica Acta, 2001Co-Authors: Rajashree A Deshpande, Ameeta Ravi Kumar, Islam M Khan, Vepatu ShankarAbstract:RNase Rs showed an approx. 2-fold increase in its activity when incubated in the presence of 2 M urea at 37 degrees C. The increase in its activity, in the presence of urea, was comparable to the activity at its Optimum Temperature, i.e. 45 degrees C. Compared to the native enzyme at 37 degrees C, the K(m) and V(max) of RNase Rs at 45 degrees C and in the presence of 2 M urea at 37 degrees C showed an increase while k(cat)/K(m) decreased. Arrhenius plots in the presence and absence of urea showed a decrease in the activation energy in the presence of urea. Though there was no change in the secondary structure of the protein in the presence of urea, minor changes were observed in the tertiary structure. Hence, the increase in the activity of RNase Rs, in the presence of 2 M urea at 37 degrees C, is due to the lowering of the activation energy as a result of changes in the microenvironment of the active site.
