User:Daniel Seeman

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''I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst''</span>
''I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst''</span>
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[[Image:delphiproteins.png|center|thumb|400px|Electrostatic potentials of β-lactoglobulin, Bovine serum albumin, and Zn-Insulin at pH 6. Calculated with DelPhi (a 'Nonlinear Poisson Boltzmann Solver') and displayed using UCSF Chimera]]
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[[Image:delphiproteins.png|center|thumb|400px|Electrostatic potentials of 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 in both protein self-association and interaction with bio-derived polyelectrolytes.]]
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Revision as of 16:51, 29 January 2014

Daniel Seeman - Department of Chemistry

I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst

Electrostatic potentials of 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 in both protein self-association and interaction with bio-derived polyelectrolytes.
Electrostatic potentials of 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 in both protein self-association and interaction with bio-derived polyelectrolytes.


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