AI Article Synopsis
- The study measures self-diffusion coefficients of globular proteins like myoglobin and lysozyme in water using NMR techniques at various temperatures and pH levels.
- The research establishes an empirical relationship for how these diffusion coefficients change with protein concentration.
- The findings are compared to the diffusion behavior of flexible polymers and rigid Brownian particles to highlight differences in their concentration dependencies.
Article Abstract
The self-diffusion coefficients of globular proteins (myoglobin, bovine serum albumin, barstar, lysozyme) in aqueous solutions at different temperatures and pH values are obtained by pulsed-gradient spin-echo NMR, and their concentration dependence is analyzed. The generalized concentration dependence of globular protein self-diffusion coefficients is empirically established, and compared to the concentration dependence of diffusion coefficients of flexible polymers and rigid Brownian particles.
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| http://dx.doi.org/10.1002/bip.10023 | DOI Listing |
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