AI Article Synopsis
- AlphaFold2 created several models of the proton/drug antiporter LmrP for the CASP competition.
- Previous research using a technique called double electron-electron resonance spectroscopy indicated that one of the less favored AlphaFold2 models might represent a structure that hasn't been captured experimentally yet.
- This suggests that computational predictions can potentially provide insights into protein structures that are challenging to determine through traditional experimental methods.
Article Abstract
As part of the CASP competition, the protein structure prediction algorithm AlphaFold2 generated multiple models of the proton/drug antiporter LmrP. Previous distance restraints from double electron-electron resonance spectroscopy, a technique which reports distance distributions between spin labels attached to proteins, suggest that one of the lower-ranked models may have captured a conformation that has so far eluded experimental structure determination.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8522053 | PMC |
| http://dx.doi.org/10.1002/prot.26138 | DOI Listing |
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