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Methyl-methane-thiosulfate-labeled cysteine and iTRAQ modification of free amine in the amino terminus and lysine were set as fixed modification.
This by-product of glycolysis induces rapid and non-enzymatic modification of free amino groups of lysine and arginine residues of proteins, leading to the generation of advanced glycation end products (AGEs) [2].
The resulting preparation containing various oxidized lipids was used to determine the modification of free amino groups in horse skeletal muscle apomyoglobin which contains one free N-terminal amino acid and 19 ε-lysyl amino group.
To determine if the active site thiols of the PDI proteins can exchange disulfides with one another, we assayed their redox status following co-incubation, by modification of free thiols with the alkylating agent AMS.
Bioconjugation via the selective modification of free cysteine in proteins has received a great deal of attention due to the unique reactivity of its thiol side chain, and the ease with which the residue can be selectively introduced via site-directed mutagenesis.
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The search parameters were: precursor ion mass tolerance of 20 p.p.m., fragment ion mass tolerance of 0.05 Da, trypsin digestion, fixed modifications of MMTS-labeled cysteine, 4-plex iTRAQ modifications of free amines at the N-termini and of lysine and variable modification 4-plex iTRAQ of tyrosine.
(39) This protocol was subsequently altered to substitute methylene chloride for chloroform in all steps with free sphinogid bases to avoid the possibility of modification of the free amine via formation of carbene in basic conditions.
Controllable modification of surface free energy and related properties (wettability, hygroscopicity, agglomeration, etc). of powders allows both understanding of fine physical mechanism acting on nanoparticle surfaces and improvement of their key characteristics in a number of nanotechnology applications.
The controllable nanoscale modification of surface free energy and related properties described in this work using low-energy electron flux is a new promising concept for nanomaterials and provides a highly potential approach for the development of new nanotechnology.
More specifically, we have demonstrated the selective modification of a free cysteine residue in a protein and also that dibromopyridazinedione 8 can be used to successfully bridge the disulfide bond of the peptide hormone somatostatin.
The influence of both kinds of stresses on the modification of the free-volume sizes in the matrix is discussed.
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