Pioneering Instrumentation for Transient Kinetics & Spectroscopy

Temperature-Jump System

Product Code:TJ-64

The system has a thermostated cell coupled directly to an optical system with absorption and fluorescence detection options. A capacitive discharge power supply is used to store the high voltage energy that is rapidly discharged into the sample.

The signal detection system incorporates fast response amplifiers and signal conditioning electronics. Data acquisition and processing is handled by Kinetic Studio, which allows the acquisition of data on linear and logarithmic time bases together with display and analysis. Multiple jumps can be set up and left to proceed in an automated manner under the management of Kinetic Studio. This turnkey solution provides a relatively straightforward and easy to use system for a technique that is traditionally only available to specialists. The sample cell has compatibility with most chemical and biological systems and can thermostated over a wide range.

We have extensive experience in the design and development of T-Jump equipment for a huge range of chemical and biological systems. For more information or copies of relevant application notes, please feel free to contact us.

Selected Publications

  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.

Application Notes

AN.019.T64

Temperature Calibration of TJ-64 Temperature-Jump Instrument using Tris/Phenol Red

AN.020.T64

Ionic Strength Dependence of the heating in TJ-64 Temperature-Jump Instrument