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By catalyzing oxidative protein folding, the bacterial disulfide bond protein A (DsbA) plays an essential role in the assembly of many virulence factors.
All PARPs catalyze the transfer of an ADP-ribose (ADPr) from NAD+ to target proteins [4] by covalently attaching ADPr to the glutamate or aspartate residues on the target proteins through an ester bond (protein mono(ADP-ribosyl)ation) [5 7].
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It served as a pulling device to detach adherent cells from protein-coated surfaces and obtain measurements of the single and multiple- bond protein-protein interactions.
In particular, we highlight the role of nonsynonymous evolution of disulphide bond proteins, the invasion antigen B (CiaB), and other secreted proteins in the determination of niche preferences.
Niche preferences can be mostly explained by nonsynonymous evolution of DSB (disulphide bond) proteins and the invasin CiaB, as well as global compositional differences in GC content, genomes size, and secretomes.
When proteins mainly interacted through medium energy interactions (disulfide bonds), protein aggregates were larger, cells walls thicker and pellets were less porous and harder with more fracture events.
The total 106 halogen bonding protein ligand complexes that were ran through both Vina and VinaXB were compared based on their RMSD values with respect to the native ligand conformation.
Our novel disulfide-bonded protein expression system on BacMPs will be useful for efficient screening of potential ligands or drugs, analyzing ligand receptor interactions or as a magnetic carrier for affinity purification.
In the absence of hydrophobic bonding, protein folding is far slower and more complex than in solution.
We computed five scores using each feature vector pairs, respectively, which included: the protein and RNA secondary structures, protein Grantham's propensities and RNA hydrogen bonding, protein Zimmerman's propensities and RNA hydrogen bonding, protein Kyte-Doolittle propensities and RNA Van der Waals' interaction, and protein Bull-Breese propensities and RNA Van der Waals' interaction.
Structural features, including structural conserved domains, disulfide bonds, protein secondary structure, residue solvent accessibility and how residues contribute to local stability (contact residues), can to some extent help in constraining the protein 3D structure.
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