User:Daniel Seeman
From Proteopedia
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- | <center>[ | + | <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: === | === About proteopedia: === | ||
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:'''<span style="color:cyan">PDB seed</span>''': automatically generated page for pdb files. | :'''<span style="color:cyan">PDB seed</span>''': automatically generated page for pdb files. | ||
:'''User pages''': ''this'' page, and others like it | :'''User pages''': ''this'' page, and others like it | ||
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- | === new page(s): === | ||
- | *[[User:Daniel Seeman/Alpha-1-antitrypsin]] | ||
- | *[[User:Daniel Seeman/Caspase-7 Dynamics]] | ||
- | *[[Alpha-1-antitrypsin]] | ||
- | *[[Molecular_Playground/BLG]] |
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.
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