Abstract
The structure of the solvent surrounding myoglobin crystals has been analyzed using neutron diffraction data, and the results indicate that the water around the protein is not disordered, but rather lies in well-defined hydration shells. We have analyzed the structure of the solvent surrounding the protein by collecting neutron diffraction data at four different temperatures, namely, 80, 130, 180, and 240K. Relative Wilson Statistics applied to low resolution data showed evidence of a phase transition in the region of 180K. A plot of the liquidity factor, Bsn, versus distance from the protein surface begins with a high plateau near the surface of the protein and drops to two minima at distances from the protein surface of about 2.35Å and 3.85Å. Two distinct hydration shells are observed. Both hydration shells are observed to expand as the temperature is increased.
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Daniels, B.V., Schoenborn, B.P., Korszun, Z.R. (1996). Myoglobin Solvent Structure at Different Temperatures. In: Schoenborn, B.P., Knott, R.B. (eds) Neutrons in Biology. Basic Life Sciences, vol 64. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5847-7_28
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DOI: https://doi.org/10.1007/978-1-4615-5847-7_28
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