SURME

                  Summer Undergraduate Research Mentored Experience

 

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Dr. Ricardo Bernal

Department of Chemistry

Biochemical and biophysical characterization of novel chaperonin protein folding mechanisms

Preferred major field of study or minimum required skills

Other than basic computer skills and having "good hands":

  • an overwhelming desire to learn science and
  • a willingness to work hard far outweigh any kind of previous lab experience or skill set.

Scholarly significance/intellectual merit

The process of protein folding is one of the most important and challenging research topics of contemporary biochemistry and in spite of its central role in life, it is one of the least understood biophysical processes. In principle, a protein’s final three-dimensional structure and function is dictated by the amino acid sequence. However, proper protein folding into the correct three-dimensional structure is influenced by a number of intracellular factors including biophysical phenomena induced by the polar solvent, molecular chaperones and by specialized macromolecular complexes termed chaperonins.

Errors in protein folding can lead to significant aggregation and severe neurodegenerative disorders such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and Amyotrophic lateral sclerosis (ALS). Therefore, it is crucial that we understand the fundamental process of protein folding in order to make significant progress into the treatment of debilitating neurodegenerative disorders.

Research question(s)

Research Questions:

  1. What are the various conformational changes that a chaperonin goes through in the process of folding a protein?
  2. What are the triggers for conformational changes in chaperonins?
  3. Do chaperonins have other activities other than the folding of proteins?
  4. Can we alter the conformational changes and therefore the the activity of the chaperonin via targeted mutations?

Methods/techniques/instruments to be learned/utilized

Computational cryo-EM reconstruction methods, dynamic light scattering (DLS) analysis, protein overexpression and purification, various chromatographic methods for protein purification, protein quantitation and analysis methods, light and electron microscopy, mass spectroscopy and various biochemical and enzymatic activity assays.

Program Coordinator



Joseph Ramos - SURME Program Coordinator

Joseph "Joe" Ramos

Campus Office of Undergraduate Research Initiatives

(915) 747-6210

josepra@utep.edu
surme@utep.edu