Using AlphaFold to predict the impact of single mutations on protein stability and function.
AlphaFold changed the field of structural biology by achieving three-dimensional (3D) structure prediction from protein sequence at experimental quality. The astounding success even led to claims that the protein folding problem is "solved". However, protein folding problem is more than ju...
Main Authors: | Marina A Pak, Karina A Markhieva, Mariia S Novikova, Dmitry S Petrov, Ilya S Vorobyev, Ekaterina S Maksimova, Fyodor A Kondrashov, Dmitry N Ivankov |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2023-01-01
|
Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0282689 |
Similar Items
-
AlphaFold2 Update and Perspectives
by: Sébastien Tourlet, et al.
Published: (2023-05-01) -
AlphaFold and the future of structural biology
by: Randy J. Read, et al.
Published: (2023-07-01) -
Using AlphaFold Predictions in Viral Research
by: Daria Gutnik, et al.
Published: (2023-04-01) -
Prediction of Monomeric and Dimeric Structures of CYP102A1 Using AlphaFold2 and AlphaFold Multimer and Assessment of Point Mutation Effect on the Efficiency of Intra- and Interprotein Electron Transfer
by: Yuri D. Ivanov, et al.
Published: (2022-02-01) -
Computational Saturation Mutagenesis to Investigate the Effects of Neurexin-1 Mutations on AlphaFold Structure
by: Raina Rhoades, et al.
Published: (2022-04-01)