Role of Hydrogen Bonds in Electron Transfer Processes of Type I Copper Proteins
Authors:
- Students:
- Maxwell Bacon
- Madelyn Dryier
- Victoria Lucarelli
- Andrew Nilsson
- Shay Parchem
- Dev Patel
- Divya Thumu
- Liyat Zekarias
- Teachers:
- Benjamin Voliva
- Maria Wilson
- Mentors:
- Sahana Sukumar (Loyola University Chicago: College of Arts and Sciences)
- Narayanasami Sukumar (Argonne National Laboratory, NE-CAT)
Advanced Photon Source Sector 24: NE-CAT
The X-ray crystal structures of several copper proteins that have been solved over the years have enhanced our current understanding in the redox enzymes. These structurally diverse groups of copper proteins perform various important biological activities, such as respiration and photosynthesis. An in depth structural bioinformatics analysis of these structures was carried out using PDB coordinates of a carefully chosen database of copper proteins to correlate the biological function of the molecules with phylogeny, hydrogen bonds, and their folding. To understand the relationship between the single crystal X-ray crystallography and structural bioinformatics and how they are intertwined with each other, we performed the structure determination of type I copper proteins along with a few model proteins like lysozyme.