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Thermal, chemical and chemothermal denaturation of yeast enolase
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| Zeitschriftentitel: | Spectroscopy |
|---|---|
| Personen und Körperschaften: | , |
| In: | Spectroscopy, 17, 2003, 2-3, S. 453-467 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Hindawi Limited
|
| Schlagwörter: |
| author_facet |
Huang, Ping Dong, Aichun Huang, Ping Dong, Aichun |
|---|---|
| author |
Huang, Ping Dong, Aichun |
| spellingShingle |
Huang, Ping Dong, Aichun Spectroscopy Thermal, chemical and chemothermal denaturation of yeast enolase Spectroscopy |
| author_sort |
huang, ping |
| spelling |
Huang, Ping Dong, Aichun 0712-4813 1875-922X Hindawi Limited Spectroscopy http://dx.doi.org/10.1155/2003/941801 <jats:p>We studied the temperature‒ and denaturant‒induced denaturation of yeast enolase by means of Fourier transform infrared spectroscopy. The temperature‒induced denaturation/aggregation of the enzyme in the absence of denaturant was highly cooperative and occurred between 55 and 65<jats:sup>°</jats:sup>C with a midpoint of ~58<jats:sup>°</jats:sup>C. Above 55<jats:sup>°</jats:sup>C, the intensity at 1656 cm<jats:sup>−1</jats:sup>(predominantly α‒helix) decreases as a function of temperature, accompanied by the appearance of two new bands at 1622 and 1696 cm<jats:sup>−1</jats:sup>, indicating the formation of intermolecular β‒sheet aggregates. Five clearly defined isosbestic points were observed, indicating a two‒state conformational transition. Addition of a non‒denaturing concentration of gdnHCl (0.4 M) caused the thermal denaturation/aggregation of the enzyme to proceed faster, but this revealed no unfolding intermediate. The gdnHCl‒induced unfolding was first detected at a gdnHCl concentration of above 0.4 M, evidenced by loss of α‒helix and β‒sheet structures as functions of denaturant concentration. The fully unfolded state was reached at a gdnHCl concentration of 1.6 M. A significant amount of intermolecular β‒sheet aggregate was detected at gdnHCl concentrations between 0.6 and 1.0 M, which disappeared as the denaturant concentration increased further. The gdnHCl‒unfolded state is a heterogeneous ensemble of turns, helix/loops, and random structures, which continues to change at higher concentrations of denaturant.</jats:p> Thermal, chemical and chemothermal denaturation of yeast enolase Spectroscopy |
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10.1155/2003/941801 |
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| title |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_unstemmed |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_full |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_fullStr |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_full_unstemmed |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_short |
Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_sort |
thermal, chemical and chemothermal denaturation of yeast enolase |
| topic |
Spectroscopy |
| url |
http://dx.doi.org/10.1155/2003/941801 |
| publishDate |
2003 |
| physical |
453-467 |
| description |
<jats:p>We studied the temperature‒ and denaturant‒induced denaturation of yeast enolase by means of Fourier transform infrared spectroscopy. The temperature‒induced denaturation/aggregation of the enzyme in the absence of denaturant was highly cooperative and occurred between 55 and 65<jats:sup>°</jats:sup>C with a midpoint of ~58<jats:sup>°</jats:sup>C. Above 55<jats:sup>°</jats:sup>C, the intensity at 1656 cm<jats:sup>−1</jats:sup>(predominantly α‒helix) decreases as a function of temperature, accompanied by the appearance of two new bands at 1622 and 1696 cm<jats:sup>−1</jats:sup>, indicating the formation of intermolecular β‒sheet aggregates. Five clearly defined isosbestic points were observed, indicating a two‒state conformational transition. Addition of a non‒denaturing concentration of gdnHCl (0.4 M) caused the thermal denaturation/aggregation of the enzyme to proceed faster, but this revealed no unfolding intermediate. The gdnHCl‒induced unfolding was first detected at a gdnHCl concentration of above 0.4 M, evidenced by loss of α‒helix and β‒sheet structures as functions of denaturant concentration. The fully unfolded state was reached at a gdnHCl concentration of 1.6 M. A significant amount of intermolecular β‒sheet aggregate was detected at gdnHCl concentrations between 0.6 and 1.0 M, which disappeared as the denaturant concentration increased further. The gdnHCl‒unfolded state is a heterogeneous ensemble of turns, helix/loops, and random structures, which continues to change at higher concentrations of denaturant.</jats:p> |
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| author | Huang, Ping, Dong, Aichun |
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| description | <jats:p>We studied the temperature‒ and denaturant‒induced denaturation of yeast enolase by means of Fourier transform infrared spectroscopy. The temperature‒induced denaturation/aggregation of the enzyme in the absence of denaturant was highly cooperative and occurred between 55 and 65<jats:sup>°</jats:sup>C with a midpoint of ~58<jats:sup>°</jats:sup>C. Above 55<jats:sup>°</jats:sup>C, the intensity at 1656 cm<jats:sup>−1</jats:sup>(predominantly α‒helix) decreases as a function of temperature, accompanied by the appearance of two new bands at 1622 and 1696 cm<jats:sup>−1</jats:sup>, indicating the formation of intermolecular β‒sheet aggregates. Five clearly defined isosbestic points were observed, indicating a two‒state conformational transition. Addition of a non‒denaturing concentration of gdnHCl (0.4 M) caused the thermal denaturation/aggregation of the enzyme to proceed faster, but this revealed no unfolding intermediate. The gdnHCl‒induced unfolding was first detected at a gdnHCl concentration of above 0.4 M, evidenced by loss of α‒helix and β‒sheet structures as functions of denaturant concentration. The fully unfolded state was reached at a gdnHCl concentration of 1.6 M. A significant amount of intermolecular β‒sheet aggregate was detected at gdnHCl concentrations between 0.6 and 1.0 M, which disappeared as the denaturant concentration increased further. The gdnHCl‒unfolded state is a heterogeneous ensemble of turns, helix/loops, and random structures, which continues to change at higher concentrations of denaturant.</jats:p> |
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| spelling | Huang, Ping Dong, Aichun 0712-4813 1875-922X Hindawi Limited Spectroscopy http://dx.doi.org/10.1155/2003/941801 <jats:p>We studied the temperature‒ and denaturant‒induced denaturation of yeast enolase by means of Fourier transform infrared spectroscopy. The temperature‒induced denaturation/aggregation of the enzyme in the absence of denaturant was highly cooperative and occurred between 55 and 65<jats:sup>°</jats:sup>C with a midpoint of ~58<jats:sup>°</jats:sup>C. Above 55<jats:sup>°</jats:sup>C, the intensity at 1656 cm<jats:sup>−1</jats:sup>(predominantly α‒helix) decreases as a function of temperature, accompanied by the appearance of two new bands at 1622 and 1696 cm<jats:sup>−1</jats:sup>, indicating the formation of intermolecular β‒sheet aggregates. Five clearly defined isosbestic points were observed, indicating a two‒state conformational transition. Addition of a non‒denaturing concentration of gdnHCl (0.4 M) caused the thermal denaturation/aggregation of the enzyme to proceed faster, but this revealed no unfolding intermediate. The gdnHCl‒induced unfolding was first detected at a gdnHCl concentration of above 0.4 M, evidenced by loss of α‒helix and β‒sheet structures as functions of denaturant concentration. The fully unfolded state was reached at a gdnHCl concentration of 1.6 M. A significant amount of intermolecular β‒sheet aggregate was detected at gdnHCl concentrations between 0.6 and 1.0 M, which disappeared as the denaturant concentration increased further. The gdnHCl‒unfolded state is a heterogeneous ensemble of turns, helix/loops, and random structures, which continues to change at higher concentrations of denaturant.</jats:p> Thermal, chemical and chemothermal denaturation of yeast enolase Spectroscopy |
| spellingShingle | Huang, Ping, Dong, Aichun, Spectroscopy, Thermal, chemical and chemothermal denaturation of yeast enolase, Spectroscopy |
| title | Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_full | Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_fullStr | Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_full_unstemmed | Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_short | Thermal, chemical and chemothermal denaturation of yeast enolase |
| title_sort | thermal, chemical and chemothermal denaturation of yeast enolase |
| title_unstemmed | Thermal, chemical and chemothermal denaturation of yeast enolase |
| topic | Spectroscopy |
| url | http://dx.doi.org/10.1155/2003/941801 |