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Hydrophobicity and molecular size are two fundamental physico-chemical properties of amino acids that determine protein structure and functionality, and naturally they greatly influence amino acid replacement rate during protein evolution [ 47].
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In this paper, we discuss a number of tools in systems engineering that would provide an analysis framework to help explain the observed dynamic behavior of the protein, ultimately making the connection between protein structure and functionality.
The effects of the mutations on protein structure and functionality were evaluated by a bioinformatic approach.
In this work protein variants characterized by mutations in functional domains of SBE enzyme have been identified and analyzed by bioinformatic tools able to predict the effect of the amino acid substitution on protein structure and functionality.
Moreover, formation of TSPs is through a single-step process of drop interaction and solidification in an aqueous solution, which represents benign conditions to preserve sensitive protein structure and functionality.
Despite the large diversity in protein structures and functionality, it is known that there are common patterns and preferences in the contacts between amino acid residues, or between residues and other biomolecules, such as DNA.
Despite the large diversity in protein structures and functionality, it is known that there are common patterns and contact preferences between residues, or even between residues and other biomolecules, such as DNA.
While lacking the transmembrane and intracellular signaling domains of VEGFR1, sVEGFR1 retains the protein structure and molecular functionality of the first six immunoglobulin-like extracellular domains of VEGFR1: i.e., an affinity for VEGF ligands, the NRP1 co-receptor, and extracellular heparan sulfate proteoglycans, as well as a capacity for homo/hetero-dimerization [13] [15].
Posttranslational modifications, such as citrullination, methylation or glycosylation, are common alterations that modify protein structure and possibly stability, functionality and antigenicity of proteins.
Since 3-dimensional protein structure and binding sites determine protein functionality, the length of the coding sequence seems to be of primary importance, and therefore the variation in the transcript length may be constrained.
We achieved a high degree of accuracy when predicting the physical properties of a protein structure, and then used two distinct methods to construct predictions of full protein structures," it adds.
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