Aysima Hacisuleyman

1 INTRODUCTION Eukaryotic cells are subdivided into numerous membrane-bound organelles, each enjoying a distinct microenvironment that enables them to carry out a particular function separate from other organelles. These organelles, such as the nuclear envelope, the endoplasmic reticulum (ER), the Golgi apparatus, lysosomes, vacuoles, endosomes, and the cell membrane, form a vast network known as the endomembrane system.

Abstract This paper presents a novel method to assess the pathogenicity of Pyrin protein mutations by using mutual information (MI) as a measure to quantify the correlation between residue motions or fluctuations and associated changes affecting the phenotype. The concept of MI profile shift is presented to quantify changes in MI upon mutation, revealing insights into residue-residue interactions at critical positions.

Abstract The amino acid sequence determines the structure, function, and dynamics of a protein. In recent years, enormous progress has been made in translating sequence information into 3D structural information using artificial intelligence. However, because of the underlying methodology, it is an immense computational challenge to extract this information from the ever increasing number of sequences.