Papers
[1] Human mitochondrial protein complexes revealed by large-scale coevolution analysis and deep learning-based structure modeling
[2] Current protein structure predictors do not produce meaningful folding pathways
[3] Harnessing protein folding neural networks for peptide-protein docking
[4] Improved prediction of protein-protein interactions using AlphaFold2
[5] AlphaFold2: A role for disordered protein prediction?
[6] AlphaFold2 transmembrane protein structure prediction shines
[7] Can AlphaFold2 predict protein-peptide complex structures accurately?
[8] Improved prediction of protein-protein interactions using AlphaFold2
[9] Possible Implications of AlphaFold2 for Crystallographic Phasing by Molecular Replacement
[10] Improved Docking of Protein Models by a Combination of Alphafold2 and ClusPro
[11] Identification of Iron-Sulfur (Fe-S) and Zn-binding Sites Within Proteomes Predicted by DeepMind’s AlphaFold2 Program Dramatically Expands the Metalloproteome
Glossary
Intrinsically Disordered Proteins (IDPs) are a large class of proteins without a rigid structure which accomplish their function despite (or thanks to) their dynamic behavior. They can become rigid in complexes with other molecules.
At the same time, it will serve as an explanation of what the sub-categories mean.