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- W2023931098 abstract "Having recently quantified how crowding can affect equilibrium protein stability (1), we have turned our attention to diffusion. Our test molecule is the small globular protein, chymotrypsin inhibitor 2. Our crowding molecules are both the synthetic polymer polyvinylpyrrolidone (PVP) and several globular proteins. We assessed both translational and rotational diffusion by using nuclear magnetic resonance spectroscopy (2). Whereas crowding by PVP results in negative deviations from the Stokes laws, crowding by globular proteins leads to positive deviations. I will discuss our results in terms of what can be learned from in vitro, versus in cell (3) studies. 1. Charlton LM, et al. (2008) Macromolecular crowding effects on protein stability at the residue level. Journal of the American Chemical Society 130: 6826-6830. 2. Li C, Wang Y, Pielak GJ (2009) Translational and rotational diffusion of a small globular protein under crowded conditions. Journal of Physical Chemistry 113: in press. 3. Slade KM, Steele BL, Pielak GJ, Thompson NL (2009) Quantifying GFP diffusion in Escherichia coli by using continuous photobleaching with evanescent illumination. Journal of Physical Chemistry 113: 4837-4845." @default.
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- W2023931098 date "2010-01-01" @default.
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- W2023931098 title "Protein Diffusion and Macromolecular Crowding" @default.
- W2023931098 doi "https://doi.org/10.1016/j.bpj.2009.12.028" @default.
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