Carbodome: Linking Carbon Distribution to Protein Stability and Function

Abstract

A novel metric Carbodome quantifies the carbon content of amino acid residues, offering insights into their hydrophobic or hydrophilic tendencies and their profound effects on protein stability and function. This study highlights key findings, demonstrating that amino acids with higher Carbodome values, such as tryptophan and phenylalanine, contribute to hydrophobic core stability, while lower Carbodome residues like arginine enhance solubility and surface interactions. The implications of carbon distribution extend to protein folding dynamics, structural integrity, and interactions, providing a foundation for advances in protein engineering, therapeutic design, and disease understanding. These findings underscore the pivotal role of carbon in shaping protein structure and functionality.