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Thermal denaturing of proteins: Equilibrium and transient studies using nonlinear infrared probes

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Ultrafast Phenomena XIV

Part of the book series: Springer Series in Chemical Physics ((CHEMICAL,volume 79))

Abstract

Thermal unfolding of β-sheets in ribonuclease A and ubiquitin is revealed by disappearance of cross peaks in 2D IR spectra. Transient unfolding probed with vibrational echoes following a temperature jump reveals nanosecond to millisecond dynamics.

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References

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Author information

Authors and Affiliations

  1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139

    H. S. Chung, M. Khalil, A. W. Smith, Z. Ganim & A. Tokmakoff

Authors
  1. H. S. Chung
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  2. M. Khalil
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  3. A. W. Smith
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  4. Z. Ganim
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  5. A. Tokmakoff
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Editor information

Editors and Affiliations

  1. Department of Physics, University of Tokyo, Hongo 7-3-1, Bunkyo, Tokyo, 113-0033, Japan

    Takayoshi Kobayashi

  2. Toyota Physical and Chemical Research Institute Nagakute, Aichi, 480-1192, Japan

    Tadashi Okada

  3. Engineering Science, Osaka University, Machikaneyama-Cho 1-3, Toyonaka, Osaka, 560-8531, Japan

    Tetsuro Kobayashi

  4. MIT Room 6-235, 77 Massachusetts Avenue, Cambridge, MA, 02139, USA

    Keith A. Nelson

  5. Dipartimento di Fisica, Politecnico di Milano, Piazza L. da Vinci 32, 20133, Milano, Italy

    Sandro De Silvestri

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© 2005 Springer-Verlag Berlin Heidelberg

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Chung, H.S., Khalil, M., Smith, A.W., Ganim, Z., Tokmakoff, A. (2005). Thermal denaturing of proteins: Equilibrium and transient studies using nonlinear infrared probes. In: Kobayashi, T., Okada, T., Kobayashi, T., Nelson, K.A., De Silvestri, S. (eds) Ultrafast Phenomena XIV. Springer Series in Chemical Physics, vol 79. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-27213-5_168

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