User:Daniel Seeman: Difference between revisions

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<center>[[User:Daniel Seeman|Daniel Seeman]]
<center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]'''
<span class="plainlinks">'''[https://people.chem.umass.edu/wiki/index.php?title=User:Dseeman My User Page on the Umass Chem Wiki]'''</span>
</center>






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

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.



About proteopedia: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