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
Current revision (19:34, 2 June 2020) (edit) (undo)
m
 
(30 intermediate revisions not shown.)
Line 1: Line 1:
-
<center>[[User:Daniel Seeman|Daniel Seeman]]
+
<center><span class="plainlinks">'''[https://www.linkedin.com/in/daniel-seeman Daniel P. Seeman, PhD (Senior Scientist)]'''
-
<br /><span class="plainlinks">'''[https://people.chem.umass.edu/wiki/index.php?title=User:Dseeman My User Page on the Umass Chem Wiki]'''
+
 
-
<br />''I am a 1st year PhD student at the University of Massachusetts Amherst Chemistry Department''</span>
+
 
-
</center>
+
 
 +
[[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: ===
Line 8: Line 13:
:'''<span style="color:green">green links'''</span>: animations/scenes
:'''<span style="color:green">green links'''</span>: animations/scenes
:'''<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
+
:'''User pages''': ''this'' page, and others like it
-
 
+
-
=== new page(s): ===
+
-
*[[/Alpha-1-antitrypsin|Alpha-1-antitrypsin]]
+

Current revision

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.
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: 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

Retrieved from "http://52.214.119.220/wiki/index.php/User:Daniel_Seeman"
Personal tools