ORBITAL PROTEIN FOLDING MODEL AND REAL TIME MUTATION DETECTION

Protein folding and Gibbs free energy are crucial for determining protein stability, but many computational models are highly complex and demand extensive computational resources. In response, the Orbital Protein Model offers a simplified alternative. This approach begins by arranging the amino acids in a circular formation. The model then proceeds to fold these residues, guiding them into a specific, organized configuration termed an "orbital structure." Within this framework, the stability of the protein can be assessed by analyzing the Gibbs free energy in relation to the diameter of the circular arrangement, providing a streamlined method for evaluating conformational stability.