Abstract
A variety of experiments, probing both static and dynamic properties of compact globular proteins such as myoglobin1–3, has provided evidence that the protein undergoes something resembling a glass transition at sufficiently low temperature, typically around 200°K. More precisely, myoglobin and several other proteins (hemoglobin, calmodulin) behave as if they possess a large number of conformational substates (CS) about a more or less fixed tertiary structure. These substates are separated by barriers whose energy scale is typically of order 200°K, the freezing temperature. Two questions which immediately come to mind are:
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1.
To what extent is the transition driven by the solvent, and to what extent is it a consequence of the internal structure of the protein itself?
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2.
How relevant are the low temperature (i.e., glassy) properties of the protein at higher, physiological temperatures?
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© 1987 Springer-Verlag Berlin Heidelberg
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Stein, D.L. (1987). Condensed Matter Biophysics: Structure and Dynamics of Large Biomolecules. In: Ehrenberg, A., Rigler, R., Gräslund, A., Nilsson, L. (eds) Structure, Dynamics and Function of Biomolecules. Springer Series in Biophysics, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71705-5_16
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DOI: https://doi.org/10.1007/978-3-642-71705-5_16
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