User:Daniel Seeman

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<center><span class="plainlinks">'''[http://www.linkedin.com/in/daniel-seeman Daniel Seeman, PhD]'''
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<center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]'''

Revision as of 19:31, 2 June 2020

Daniel P. Seeman, PhD (Senior Scientist)


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.
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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