BOC Sciences adopts advanced technology, focuses on the custom synthesis and detection and analysis of amino acids, and provides customers with professional amino acid protonation, deprotonation and isoelectric point determination services.
Amino acids are the basic units of protein synthesis. Amino acids are amphoteric due to the simultaneous presence of amino and carboxyl groups in the molecule. When the acidity and alkalinity in the biological fluid deviate from the optimal condition of biological activity, amino acid molecules will automatically accept protons or release protons to maintain the acid-base balance in the organism and the biological activity of proteins. Therefore, the protonation reaction of amino acids is of great significance to life science.
The main form of ions of amino acids
Protonation reactions are the process by which atoms, molecules or ions gain protons. The reverse process of protonation is deprotonation. Amino acids are amphoteric substances, and both their amino and carboxyl groups can undergo protonation reactions. Protonation of amino groups is an effective means of protecting amino acids and can be used in solid-phase synthesis of peptides. Protonation prediction is important for the accuracy of predicting molecular docking of drugs and substrates within the binding site and for traditional molecular dynamics studies. We provide comprehensive solutions for protonation and deprotonation protection, protonation prediction, and isoelectric point determination of amino acids. In addition, based on efficient services, we also synthesize high-quality and cheap free amino acids, protected amino acids, peptides and their derivatives, and can provide related homology modeling and MD research services.
The protonation reaction of amino acid can protect its amino group from being oxidized and change the positioning effect of the substitution reaction, which is the simplest amino group protection method.
In protein homology modeling, the protonation of amino acids needs to be considered. Protonation of side chains plays a role in the majority of hydrogen donors and/or hydrogen acceptors and electrostatic interactions in proteins and can affect the accuracy of computational predictions. Protonation is affected by the surrounding environment (e.g. pH, temperature, neighboring residues). Protonation and deprotonation of amino acids will lead to electrostatic interactions on the side chains of proteins. Our computational team estimates pK constants to predict protonation from studies in electrostatics and molecular mechanics.
The isoelectric point of an amino acid is the pH value of the amino acid under specific conditions. At this time, the positive and negative charges of the amino acid have the same number, and the protonation tendency is equal to the deprotonation tendency. Various amino acids have different isoelectric points due to their different compositions and structures. Based on capillary isoelectric focusing (cIEF) technology, we can realize the determination of the isoelectric point of any amino acid. Our assay has the advantages of short time-consuming, high efficiency, high precision, and less sample usage. Through the determination of the isoelectric point of amino acids, the weak acidity and strong alkalinity of proteins can be accurately analyzed, and the charge and stability of amino acids can be determined, which has a profound impact on the determination of protein structure.