This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


User:Daniel Seeman

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
''I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst''</span>
''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 β-lactoglobulin, Bovine serum albumin, and Zn-Insulin at pH 6. Calculated with DelPhi (a 'Nonlinear Poisson Boltzmann Solver') and displayed using UCSF Chimera]]
+
[[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. Protein charge anisotropy is a major component in both protein self-association and interaction with bio-derived polyelectrolytes.]]
</center>
</center>

Revision as of 16:51, 29 January 2014

Daniel Seeman - Department of Chemistry

I am a Ph.D. Candidate in the Dubin Research Group at the University of Massachusetts-Amherst

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. Protein charge anisotropy is a major component in both protein self-association and interaction with bio-derived polyelectrolytes.
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. Protein charge anisotropy is a major component in both protein self-association and interaction with bio-derived polyelectrolytes.


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

Proteopedia Page Contributors and Editors (what is this?)

Daniel Seeman, Eric Martz

Personal tools