Programs Faculty Opportunities Facilities

Dr. Tara Phelps-Durr

TaraPhelps-Durr

Associate Professor
Curie Hall 0234
Box 6931, Radford University
Radford, VA 24142-6939, U.S.A.
Tel:(540) 831-5714
E-mail: tphelpsdu@radford.edu

Courses Taught:

  • Biology 160 - Freshman Seminar in Biology
  • Biology 231 - Genetics, Evolution and Development
  • Biology 430 - Genes and Development
  • Biology 460 - Advanced Seminar in Biology
  • Biology 491 - Independent Research

About:

My lab works with several genes that are required for normal plant development. Specifically, the three dimensional structures of the proteins encoded by these genes are analyzed to determine how they interact with other proteins and/or regulatory regions of DNA. Some students in the lab perform biochemical and molecular biology experiments while others computationally analyze protein structure using molecular modeling and simulation software.

Available projects  

1. Perform biochemical assays to verify protein-protein interactions.

2. Clone various genes such that the proteins encoded by these genes can be isolated and crystallized. Ultimately, this will be used to determine three dimensional structure of the protein (in collaboration with Dr. Kimberly Lane). 

3. Computationally analyze proteins using ICM-Pro to determine if the proteins interact in silico (In collaboration with Drs. Kimberly Lane and Timothy Fuhrer).

4. Computationally analyze proteins to determine if and how the proteins interact with DNA (In collaboration with Drs. Kimberly Lane and Timothy Fuhrer).

Those who are interested in molecular modeling are encouraged to download the free ICM-Browser software (http://www.molsoft.com/icm_browser.html) and open this file (for best results on a PC, right-click to "save target as"). Once the file is open, users can visualize and manipulate the protein structure model in the file and get a sense of what it is like to work with computational modeling software.

 

TaraPhelpsDurrModel

Figure 1 -Computational models of the interaction between the ASYMMETRIC LEAVES 1 (black) and ASYMMETRIC LEAVES2 (gray) proteins. A) Ribbon model. B) Space filling model.