Keywords

Thermodynamic properties, X-ray crystallography, Enzymes, Nuclear magnetic resonance, Amino acid, Lysozyme, Proteins, Biotechnology, Mutagenesis, Viruses

Abstract

Protein surface interactions are important in many applications in biotechnology including protein arrays, but these technologies have not lived up to their transformative potential because it is difficult to attach proteins to surfaces in a manner that preserves function and theoretical understanding of the relevant phenomena remains limited. Here is reported the effect of using multiple tethers to attach a protein (lysozyme) to a surface and the effects on the structure and stability of the molecule. The simulations show how using two tethers can drastically change the folding mechanism such that a protein that is initially unstable and inactive when attached using a single tether can become more stable and functional when two tethers are used. The results offer hope that the rational design of protein arrays is possible.

Original Publication Citation

B. K. Loong and T. A. Knotts IV, Communication: Using Multiple Tethers to Stabilize Proteins on Surfaces, J. Chem. Phys., 141, 051104 (2014).