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User:Daniel Seeman
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| - | <center><span class="plainlinks">'''[https:// | + | <center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]''' |
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| + | [[Image:delphiproteins.png|center|thumb|400px|Electrostatic potentials of three proteins (β-lactoglobulin, Bovine serum albumin, and Zn-Insulin) at pH 6. Calculated with DelPhi (a 'Nonlinear Poisson Boltzmann Solver') and displayed using UCSF Chimera. Protein charge anisotropy is a major component of both protein self-association, ''and'' interactions with bio-derived polyelectrolytes.]] | ||
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| - | [[Image:delphiproteins.png|Y. Xu, D. Seeman, Y. Yan, L. Sun, J. Post, P.L. Dubin. “Effect of Heparin on Protein Aggregation: Inhibition versus Promotion”. Biomacromolecules, 13 (2012), 1642-1651]] | ||
=== About proteopedia: === | === About proteopedia: === | ||
Current revision
Electrostatic potentials of three proteins (β-lactoglobulin, Bovine serum albumin, and Zn-Insulin) at pH 6. Calculated with DelPhi (a 'Nonlinear Poisson Boltzmann Solver') and displayed using UCSF Chimera. Protein charge anisotropy is a major component of both protein self-association, and interactions with bio-derived polyelectrolytes.
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