They combined this technique with a computational investigation led by Professor Turkan Haliloglu, which allows scientists to develop models and simulations-based data—in this case predicting how a molecule might react and mutate following biochemical changes and how this might affect the progression of a disease.
Being able to identify such mutations would allow scientists to understand mutation-led diseases such as cancer and cystic fibrosis, as well as design more effective drugs to treat or vaccinate against these diseases, and even COVID-19 in the future.
Speaking about the research, Dr. Torun said: “This is the first time that these two techniques of experimental investigation and computational investigation have been combined to examine a specific protein molecule.
“Isolating one particular molecule in this way is not common practice, but it is the most effective way to probe the structure of the molecule and ask questions such as ‘what if I change a specific part of the protein?’ or ‘what if I attach a specific enzyme to the protein?’
“This research has huge potential for application, and we hope it will lead to new breakthroughs in the treatment of diseases in the future.”
Saliha Ece Acuner et al. Oncogenic mutations on Rac1 affect global intrinsic dynamics underlying GTP and PAK1 binding, Biophysical Journal (2021). DOI: 10.1016/j.bpj.2021.01.016
Protein dynamics research breakthrough could result in new cancer treatments (2021, March 26)
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