User:Daniel Seeman
From Proteopedia
(Difference between revisions)
m |
|||
(39 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | <center | + | <center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]''' |
- | + | ||
- | + | ||
- | + | ||
+ | [[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: === | === About proteopedia: === | ||
- | :'''Topic Pages''' | + | :'''<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 |
Current revision

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