User:Daniel Seeman: Difference between revisions

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<center><span class="plainlinks">'''[https://people.chem.umass.edu/dseeman/ Daniel Seeman - Department of Chemistry]'''
<center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]'''
''I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst''</span>
 
 
 
[[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.]]


[[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]]


</center>




Latest revision as of 22:34, 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.



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