Utilization of Hydrophobic Microenvironment Sensitivity in Diethylpyrocarbonate Labeling for Protein Structure Prediction.

ABSTRACT: Diethylpyrocarbonate (DEPC) labeling analyzed with mass spectrometry can provide important insights into higher order protein structures. It has been previously shown that neighboring hydrophobic residues promote a local increase in DEPC concentration such that serine, threonine, and tyrosine residues are more likely to be labeled despite low solvent exposure. In this work, we developed a Rosetta algorithm that used the knowledge of labeled and unlabeled serine, threonine, and tyrosine residues and assessed their local hydrophobic environment to improve protein structure prediction. Additionally, DEPC-labeled histidine and lysine residues with higher relative solvent accessible surface area values (i.e., more exposed) were scored favorably. Application of our score term led to reductions o

SUBMITTER: Biehn SE 

PROVIDER: S-EPMC8336574 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature