pKa
As applications, we have derived the p K a value of the side chain of an amino acid and almost reproduced the experimental value. By using our computing schemes, we showed the influence of hydrogen bonds on the p K a values in the case of tripeptides, which decreases the p K a value...
It was also possible to determined the p K a values some amino acids containing ionizable side-chains. This study shows that, in order to understand fully the retention behaviour of peptides containing an α-amino group in reversed-phase chromatography, one must incorporate an α-amino group ...
Accuracy of Density Functionals in the Prediction of Electronic Proton Affinities of Amino Acid Side Chains The ionization states of amino acids influence the structure, function, stability, solubility, and reactivity of proteins and are difficult to determine un... NF Brás,MAS Perez,PA Fernandes,...
M. Addition of "charge-shifting" side chains to liner poly(ethyleneimine) enhances cell transfection efficiency. Biomacromolecules 9, 2063–2071 (2008). 8. Shao, Q. & Jiang, S. Molecular understanding and design of zwitterionic materials. Adv. Mater. 27, 15–26 (2015). 9. Xie, J. & ...
3 A). The S-AKAP84 sequence contains amino acids with large hydrophobic side chains that align in perfect register with six Leu, Ile, and Val residues that are critical for high-affinity binding of RII and PKA isoforms by AKAP75 (7). Potential boundaries for the S-AKAP84 tethering site...
Under these conditions, due to variable pKa values of individual lysine side chains in the protein of interest different levels of lysine protonation are observed. These differences are reflected in the chemical shift differences of methyl groups in reductively methylated lysines. We show that this ...
The fluorescence lifetime of Dbo in the peptides ( τ ) was measured as a function of pH. The side chains collide with Dbo intramolecularly and quench it efficiently only when they are deprotonated (i.e., pH≥side chain p K a ). The p K a values of the H 6 , K 6 , and R ...
This is the largest pKa shift for an A residue in structured nucleic acids reported so far, and similar in size to the largest pKa shifts observed for amino acid side chains in proteins. Both RNA pre-folding and ligand binding contribute to the pKa shift.Wiley...
On the other hand, HC∗-CDR3-Lys98 is facing toward the side chains of Asp112 and can potentially form a salt bridge with the carboxyl group on Asp112 (only 1.8 Å away). Because of the nature of the local environment, it is possible that HC-CDR3-Lys98 may have more flexibility...