Errors Made in Ab Initio+ Homology-based Protein Structure Prediction Tools Arise Due to Lack of Consideration of Impact Forces

There is a requirement for accurate tertiary structure prediction to understand a protein’s conformation. Forces like electrostatic and Van der Waals interaction, hydrogen bonds and hydrophobic interaction are often considered when it comes to tertiary structure modelling by computer algorithms. Even though the resulting structure is well modelled and shows some resemblance to native structures, it always permits slight inaccuracies at very low resolutions. Until now, no algorithm has efficiently predicted protein structures with 100% accuracy. With the advent of modern medical technologies such as precision medicine, we require highly resolved protein structures predicted to almost 100% accuracy. The specificity of structures accounts for the various protein functions, protein interaction networks, their mutations, and how the mutation cause diseases. Variations in the sequence will, in turn, affect protein functionality and their pathways. Thus, the structure of the encoded protein, as well as its mutations, can provide a full understanding of the pathogenesis, targeted therapies and additionally, potential strategies for drug development based on molecular structure. The success of structure-based targeted drug therapy relies heavily on the availability of accurate 3D structures. For this, detailed knowledge of protein structure at the atomic level of resolution is required.