Where to From Here?

Front Mol Biosci

Department of Molecular and Cell Biology, Centro de Investigaciones Biológicas Margarita Salas, CSIC, Madrid, Spain.

Published: March 2022

The biological-biochemical community has been shocked and delighted by the remarkable progress that has recently been made on a problem that has consumed the attention, energy, and resources of many, if not most of the scientists in the field for the past 50 years. The problem has been to predict the tertiary structure of a protein merely from its amino acid sequence. Nature does it easily enough, but it has been an incredibly difficult problem, often considered intractable, for humankind. The breakthrough has come in the form of two computer-based approaches, AlphaFold2 and RoseTTAFold in conjunction with factors such as the use of vast computing power, the field of artificial intelligence, and the existence of huge protein sequence databases. The advancement of these tools depended upon and was stimulated by the last 50 years of development of smaller and smaller and more and more powerful electronics components, mainly processors and memory. Along with the problem of protein folding, determining the function or mechanism of action of proteins has similarly limped along as did protein folding until the recent breakthroughs. Perhaps AlphaFold2 and RoseTTAFold can substantially aid in protein mechanistic studies. Now it is not completely insane to consider what might be the next grand challenge in biochemistry-biology. We offer several possibilities.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8990317PMC
http://dx.doi.org/10.3389/fmolb.2022.848444DOI Listing

Publication Analysis

Top Keywords

alphafold2 rosettafold
8
protein folding
8
protein
5
here? biological-biochemical
4
biological-biochemical community
4
community shocked
4
shocked delighted
4
delighted remarkable
4
remarkable progress
4
problem
4

Similar Publications

Challenge for Deep Learning: Protein Structure Prediction of Ligand-Induced Conformational Changes at Allosteric and Orthosteric Sites.

J Chem Inf Model

November 2024

Medicinal Chemistry, Research and Early Development, Respiratory and Immunology (R&I), BioPharmaceuticals R&D, AstraZeneca, 43183 Gothenburg, Sweden.

In the realm of biomedical research, understanding the intricate structure of proteins is crucial, as these structures determine how proteins function within our bodies and interact with potential drugs. Traditionally, methods like X-ray crystallography and cryo-electron microscopy have been used to unravel these structures, but they are often challenging, time-consuming and costly. Recently, a breakthrough in computational biology has emerged with the development of deep learning algorithms capable of predicting protein structures based on their amino acid sequences (Jumper, J.

View Article and Find Full Text PDF

Histones and histone variant families in prokaryotes.

Nat Commun

September 2024

Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands.

Histones are important chromatin-organizing proteins in eukaryotes and archaea. They form superhelical structures around which DNA is wrapped. Recent studies have shown that some archaea and bacteria contain alternative histones that exhibit different DNA binding properties, in addition to highly divergent sequences.

View Article and Find Full Text PDF

AI-Driven Deep Learning Techniques in Protein Structure Prediction.

Int J Mol Sci

August 2024

College of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.

Protein structure prediction is important for understanding their function and behavior. This review study presents a comprehensive review of the computational models used in predicting protein structure. It covers the progression from established protein modeling to state-of-the-art artificial intelligence (AI) frameworks.

View Article and Find Full Text PDF

Artificial intelligence in fusion protein three-dimensional structure prediction: Review and perspective.

Clin Transl Med

August 2024

Department of Bioinformatics and Systems Medicine, McWilliams School of Biomedical Informatics, The University of Texas Health Science Center at Houston, Houston, Texas, USA.

Recent advancements in artificial intelligence (AI) have accelerated the prediction of unknown protein structures. However, accurately predicting the three-dimensional (3D) structures of fusion proteins remains a difficult task because the current AI-based protein structure predictions are focused on the WT proteins rather than on the newly fused proteins in nature. Following the central dogma of biology, fusion proteins are translated from fusion transcripts, which are made by transcribing the fusion genes between two different loci through the chromosomal rearrangements in cancer.

View Article and Find Full Text PDF

Structures prediction and replica exchange molecular dynamics simulations of α-synuclein: A case study for intrinsically disordered proteins.

Int J Biol Macromol

September 2024

Turkish-German University, Molecular Biotechnology, Sahinkaya Caddesi, No. 106, Beykoz, Istanbul 34820, Turkey. Electronic address:

In recent years, a variety of three-dimensional structure prediction tools, including AlphaFold2, AlphaFold3, I-TASSER, C-I-TASSER, Phyre2, ESMFold, and RoseTTAFold, have been employed in the investigation of intrinsically disordered proteins. However, a comprehensive validation of these tools specifically for intrinsically disordered proteins has yet to be conducted. In this study, we utilize AlphaFold2, AlphaFold3, I-TASSER, C-I-TASSER, Phyre2, ESMFold, and RoseTTAFold to predict the structure of a model intrinsically disordered α-synuclein protein.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!