User:Daniel Seeman: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Update current affiliation/title
mNo edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
<center><span class="plainlinks">'''[linkedin.com/in/daniel-seeman Daniel Seeman, PhD]'''
<center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]'''




Line 5: Line 5:
[[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 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.]]


</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.



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