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• W2884028105 abstract "It is known that the crystallizability of protein molecules may be improved by replacing their surface lysine residues with other residue types. Here an experimental method to identify surface lysine residues by NHS-biotin chemical modification combined with MALDI-TOF MS was proposed and was evaluated using PH1033 protein from Pyrococcus horikoshii. Interestingly, the biotinylation experiment with a protein-reagent molar ratio of 1:1 revealed that only seven of twenty-two lysine residues in the protein comprising 144 residues were labeled. To investigate the result, we analyzed structures from a molecular-dynamics simulation mimicking the experiment. A logistic regression analysis revealed that the biotinylation was significantly correlated with four factors relevant to the local environment of lysine residues: the solvent accessibility, the electrostatic energy, the number of hydrogen bonds, and the estimated pKa value. This result is overall in agreement with that from the same analysis on the crystal structure. However, reflecting the flexibility of the protein molecule in solution state, the factors except for the electrostatic energy were highly variable in the MD structures depending upon the protonation state of Tyr87. The present procedure of biotin-labeling can avoid lysine residues with extensive intramolecular interactions that are incompatible with the rational design of protein crystals." @default.
• W2884028105 created "2018-08-03" @default.
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• W2884028105 date "2018-09-01" @default.
• W2884028105 modified "2023-09-26" @default.
• W2884028105 title "Availability of NHS-biotin labeling to identify free protein lysine revealed by experiment and MD simulation" @default.
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• W2884028105 doi "https://doi.org/10.1016/j.ab.2018.07.009" @default.
• W2884028105 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30025973" @default.
• W2884028105 hasPublicationYear "2018" @default.
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