Paper
1 December 1989 Temperature Dependences Of The Infrared And Circular Dichroism Spectra Of Ribonuclease A And Troponin C
Tatsuyuki Yamamoto, Masaru Tanokura, Mitsuo Tasumi
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Proceedings Volume 1145, 7th Intl Conf on Fourier Transform Spectroscopy; (1989) https://doi.org/10.1117/12.969455
Event: Seventh International Conference on Fourier and Computerized Infrared Spectroscopy, 1989, Fairfax, VA, United States
Abstract
Temperature dependences of the infrared and CD spectra of bovine pancreatic ribonuclease A and bullfrog skeletal muscle troponin C have been examined. In order to extract information on the secondary structure changes of these proteins from their infrared spectra, the methods of difference spectrum and Fourier-self-deconvolution have been applied. Both the infrared and circular dichroism spectra have confirmed that ribonuclease A undergoes thermal denaturation at 60°C in a typical manner. On the contrary, calcium-free troponin C shows gradual spectral changes with increasing temperature, indicating the absence of drastic conformational changes. No denaturation seems to take place for calcium-bound toponin C even at 80°C.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Tatsuyuki Yamamoto, Masaru Tanokura, and Mitsuo Tasumi "Temperature Dependences Of The Infrared And Circular Dichroism Spectra Of Ribonuclease A And Troponin C", Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); https://doi.org/10.1117/12.969455
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KEYWORDS
Infrared radiation

Proteins

Dichroic materials

Temperature metrology

Thermography

Transmission electron microscopy

Calcium

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