Correlation Function for Heteropolymers Near the Melting Temperature

Abstract

The stability of heterogeneous biopolymers is extremely important for maintaining their conformation and carrying out biological functions. The conformational stability of these molecules determines their ability to preserve the necessary structure for biological processes such as catalytic activity, molecular recognition, and cellular interactions. Within the framework of the Generalized Model of the Polypeptide Chain (GMPC), the correlation function of a two-component heteropolymer has been computed as a function of distance, specifically the number of repeating units between two monomers in a helical state, using the method of super-matrices. Through this research, dependencies of the correlation function on the number of repeating units between monomers in the helical state have been obtained for several realizations and different temperatures, particularly around the melting temperature. An interpolation dependency has been proposed for the curve at the melting temperature, expressed as a sum of exponential and power functions. This model allows for a more accurate description of the correlation function behavior under critical conditions close to the melting temperature. The exponential part of the model reflects intense decay of correlation at short distances, while the power function describes mild changes at longer distances.