產品資訊

動力學實驗儀器 快速變溫採集系統

快速變溫實驗系統

該系統具有一個恆溫樣品池,該恆溫樣品池直接耦合到具有吸收光譜和螢光光譜檢測選項的光學系統。電容性放電電源用於存儲迅速釋放到樣品中的高壓能量。 信號檢測系統集成了快速響應放大器和信號調節電子設備。使用Kinetic Studio進行數據採集和處理,它允許在線性時基和對數時基上進行數據採集以及顯示和分析。可以設置多個跳轉,並在Kinetic Studio的管理下以自動方式進行跳轉。這種統整解決技術提供了一個相對簡單易用的系統。樣品池與大多數化學和生物系統兼容,並且可以在很寬的範圍內進行恆溫。 我們在為各種化學和生物系統設計和開發此類T-Jump設備方面擁有豐富的經驗。有關更多信息或相關應用,請隨時與我們聯繫。 參考出版期刊 Gianni, S., Morrone, A., Giri, R. and Brunori, M. (2012) A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein. Biochemical and Biophysical Research Communications, 428, Issue 2, 16 November 2012, pp. 205-209. Giri, R., Morrone, A., Travaglini-Allocatelli, C., Jemth, P., Brunori, M. and Gianni, S. (2012) Folding pathways of proteins with increasing degree of sequence identities but different structure and function. PNAS, Early Edition. Dodson, C.A., Ferguson, N., Rutherford, T.J., Johnson, C.M. and Fersht, A. (2010) Engineering a two-helix bundle protein for folding studies. Protein Engineering, Design & Selection, 23, no. 5, pp. 357-364. Neuweiler, H., Johnson, C.M. and Fersht, A. (2009) Direct Observation of ultrafast folding and denatured state dynamics in single protein molecules. PNAS, November 3, 106, no. 44, pp. 18569-18574. Hart, T., Hosszu, L.L.P., Trevitt, C.R., Jackson, G.S., Waltho, J.P., Collinge, J. and Clarke, A.R. (2009) Folding kinetics of the human prion protein probed by temperature jump. PNAS, April 7, 106, no. 14, pp. 5651-5656.


該系統具有一個恆溫樣品池,該恆溫樣品池直接耦合到具有吸收光譜和螢光光譜檢測選項的光學系統。電容性放電電源用於存儲迅速釋放到樣品中的高壓能量。

信號檢測系統集成了快速響應放大器和信號調節電子設備。使用Kinetic Studio進行數據採集和處理,它允許在線性時基和對數時基上進行數據採集以及顯示和分析。可以設置多個跳轉,並在Kinetic Studio的管理下以自動方式進行跳轉。這種統整解決技術提供了一個相對簡單易用的系統。樣品池與大多數化學和生物系統兼容,並且可以在很寬的範圍內進行恆溫。

我們在為各種化學和生物系統設計和開發此類T-Jump設備方面擁有豐富的經驗。有關更多信息或相關應用,請隨時與我們聯繫。

參考出版期刊

  1. Gianni, S., Morrone, A., Giri, R. and Brunori, M. (2012) A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein. Biochemical and Biophysical Research Communications, 428, Issue 2, 16 November 2012, pp. 205-209.
  2. Giri, R., Morrone, A., Travaglini-Allocatelli, C., Jemth, P., Brunori, M. and Gianni, S. (2012) Folding pathways of proteins with increasing degree of sequence identities but different structure and function. PNAS, Early Edition.
  3. Dodson, C.A., Ferguson, N., Rutherford, T.J., Johnson, C.M. and Fersht, A. (2010) Engineering a two-helix bundle protein for folding studies. Protein Engineering, Design & Selection, 23, no. 5, pp. 357-364.
  4. Neuweiler, H., Johnson, C.M. and Fersht, A. (2009) Direct Observation of ultrafast folding and denatured state dynamics in single protein molecules. PNAS, November 3, 106, no. 44, pp. 18569-18574.
  5. Hart, T., Hosszu, L.L.P., Trevitt, C.R., Jackson, G.S., Waltho, J.P., Collinge, J. and Clarke, A.R. (2009) Folding kinetics of the human prion protein probed by temperature jump. PNAS, April 7, 106, no. 14, pp. 5651-5656.