Abstract: Genome sequencing initiatives have significantly expanded the range of protein sequences that we can study, enabling comprehensive studies of complex biological systems and microenvironments. While genome data can provide insights into the functional aspects of complex biological systems, we must also rely on structural observations to more comprehensively understand them. Advances in structural biology, like the development of new X-ray synchrotron facilities with dedicated protein crystallography beamlines, have greatly improved our ability to determine protein structures.
Additionally, world-wide Structural Genomics efforts, which utilize a range of cost-effective methods in bioinformatics, molecular biology, proteomics, and crystallization, have created efficient pipelines for structure determination. Cryo-electron microscopy (Cryo-EM) has expanded the range of experimental structures that can be determined, including large, multi-component assemblies.
Public databases, containing a large number of unique protein structures, have allowed for the development of new, highly sophisticated algorithms (AlphaFold, Rosetta) for ab initio structure prediction, which strongly complement experimental efforts. The shared knowledge and understanding of biological mechanisms that is made available through public databases can inform the development of novel biological functions, as well as help us understand the evolution of biological systems and design synthetic ones. Thanks to advances in synchrotrons, supercomputing, and artificial intelligence, the pace of our understanding of biology may achieve new dimensions. Although there are still challenges to be addressed, the potential solutions and future advances in these areas will continue to be discussed.