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Most native proteins do not make optimal drugs and thus a second- and third-generation of therapeutic proteins, which have been engineered to improve product attributes or to enhance process characteristics, are rapidly becoming the norm.
Most native proteins will partition into the dextran-rich phase.
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Together, these data suggest that α3D, although folded into a unique three-dimensional structure, is nevertheless more malleable and flexible than most natural, native proteins.
In contrast to HSP47, most other chaperones destabilize native proteins by preferential binding to unfolded, partially unfolded, and misfolded polypeptide chains.
Beta-sheet in native proteins has at most four layers of sheet and less than 300 amino acid residues, while amyloid and α-sheet have multiple layers and typically thousands of residues or more.
The addition of a new function to native proteins is one of the most attractive protein-based designs.
In E. coli only a minority of the native proteins contains a flavin cofactor and most of them will not be reactive with NADPH.
To what extent can inter-residue contact predictions from multiple sequence alignments, information which is orthogonal to that used in most structure prediction algorithms, be used to identify those models most similar to the native protein structure?
Nonetheless, the fact that 17G1 recognized native forms of PSMA is most valuable in the context of molecular imaging whereby intravenously injected radiotracers recognize accessible epitopes in native proteins.
However, when it comes to unfolded native proteins, or to short polypeptides, evidence [ 31] suggests that PPII is the most common conformation.
Antibodies targeted against mutant proteins are the most direct explanation for the stimulation of an immune response, and the antibodies may well exhibit cross-reactivities with native proteins.
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