Browsing 002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences by Subject "lysine"
Now showing items 1-8 of 8
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Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
(2007)Modifications on histones control important biological processes through their effects on chromatin structure. Methylation at lysine 4 on histone H3 (H3K4) is found at the 5′ end of active genes and contributes to ...
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A correction to the calculation of the Gibbs free energy of adsorption for biomolecules in ion-exchange systems
(1997)We wish to propose a correction to the methodology introduced by Gerstner et al. [J.A. Gerstner, J.A. Bell, S.M. Cramer, Biophys. Chem. 52 (1994) 97-106] for the calculation of Gibbs free energies of adsorption of biomolecules ...
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N-alpha-terminal Acetylation of Histone H4 Regulates Arginine Methylation and Ribosomal DNA Silencing
(2013)Post-translational modifications of histones play a key role in DNA-based processes, like transcription, by modulating chromatin structure. N-terminal acetylation is unique among the numerous histone modifications because ...
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The Polycomb Group Protein SUZ12 regulates histone H3 lysine 9 methylation and HP1α distribution
(2007)Regulation of histone methylation is critical for proper gene expression and chromosome function. Suppressor of Zeste 12 (SUZ12) is a requisite member of the EED/EZH2 histone methyltransferase complexes, and is required ...
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Proton binding to proteins: A free-energy component analysis using a dielectric continuum model
(2005)Proton binding plays a critical role in protein structure and function. We report pKa calculations for three aspartates in two proteins, using a linear response approach, as well as a "standard" Poisson-Boltzmann approach. ...
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Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27
(2004)Polycomb group (PcG) complexes 2 and 3 are involved in transcriptional silencing. These complexes contain a histone lysine methyltransferase (HKMT) activity that targets different lysine residues on histones H1 or H3 in ...
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Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations
(1998)Specific amino acid binding by aminoacyl-tRNA synthetases is necessary for correct translation of the genetic code. To obtain insight into the origin of the specificity, the binding to aspartyl-tRNA synthetase (AspRS) of ...
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