Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: divides amino acids to two groups: hydrophobic (H) and polar (P), and considers only hydrophobic interactions beten neighboring H amino in the energy formula. Another significant force acting during the protein folding are sulfide (SS) bridges beten two cysteine amino acids. ,  will enrich the HP model by adding cysteines as the third group of amino acids. A cysteine monomer acts as an H amino acid, but in addition two neighboring cysteines can form a bridge to further reduce the energy of the fold.  call our model the HPC model.  consider a subclass of linear structures designed in Gupta et al. 1 which is rich enough to approximate (although more coarsely) any given structure.  refine the structures for the HPC model by setting approximately a half of H amino acids to cysteine ones.  conjecture that these structures are stable under the HPC model and prove it under an additional assumption that non-cysteine amino acids act as cysteine ones, i.e., they tend to form their own bridges to reduce the energy. In the proof  will make an efficient use of a computational tool 2DHPSolver which significantly speeds up the progress in the technical part of the proof. This is a preliminary work, and  believe that the same techniques can be used to prove this result without the artificial assumption about non-cysteine H monomers.
['Alireza Hadj Khodabakhshi', 'Ján Manuch', 'Arash Rafiey', 'Arvind Gupta']
I am writing a research paper on a idea Structure-approximating design of stable proteins in 2D HP model fortified by cysteine monomers
[{"from": "human", "value": "I am writing a research paper on a idea Structure-approximating design of stable proteins in 2D HP model fortified by cysteine monomers"}, {"from": "gpt", "value": "Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: divides amino acids to two groups: hydrophobic (H) and polar (P), and considers only hydrophobic interactions beten neighboring H amino in the energy formula. Another significant force acting during the protein folding are sulfide (SS) bridges beten two cysteine amino acids. ,  will enrich the HP model by adding cysteines as the third group of amino acids. A cysteine monomer acts as an H amino acid, but in addition two neighboring cysteines can form a bridge to further reduce the energy of the fold.  call our model the HPC model.  consider a subclass of linear structures designed in Gupta et al. 1 which is rich enough to approximate (although more coarsely) any given structure.  refine the structures for the HPC model by setting approximately a half of H amino acids to cysteine ones.  conjecture that these structures are stable under the HPC model and prove it under an additional assumption that non-cysteine amino acids act as cysteine ones, i.e., they tend to form their own bridges to reduce the energy. In the proof  will make an efficient use of a computational tool 2DHPSolver which significantly speeds up the progress in the technical part of the proof. This is a preliminary work, and  believe that the same techniques can be used to prove this result without the artificial assumption about non-cysteine H monomers."}]