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User:Daniel Seeman

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I am a 1st year PhD student at the University of Massachusetts Amherst Chemistry Department.
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<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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=== About proteopedia: ===
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:'''<span style="color:blue">Topic Pages'''</span>: articles
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:'''<span style="color:green">green links'''</span>: animations/scenes
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:'''<span style="color:cyan">PDB seed</span>''': automatically generated page for pdb files.
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:'''User pages''': ''this'' page, and others like it

Current revision

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.



About proteopedia:

Topic Pages: articles
green links: animations/scenes
PDB seed: automatically generated page for pdb files.
User pages: this page, and others like it

Proteopedia Page Contributors and Editors (what is this?)

Daniel Seeman, Eric Martz

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