Why arginine is basic

Sign up or log in Sign up using Google. Sign up using Facebook. Sign up using Email and Password. Post as a guest Name. Email Required, but never shown. Featured on Meta. Now live: A fully responsive profile. Version labels for answers. Related 5. Hot Network Questions. Question feed. Chemistry Stack Exchange works best with JavaScript enabled. The number of protons is also referred to as the "atomic number," abbreviated Z.

Elements are ordered by increasing atomic number in the periodic table of elements. The pKa is the flipping power needed to flip half the coins. Amino acids are this weak kind. But when amino acids link together to form peptides and proteins, they do so using those groups. But some amino acids have an additional site that can still act as an acid. The " of charges" is referred to as the valency.

Negatively-charged ions are attracted to one another and can form strong non-covalent bonds called "ionic bonds" or "salt bridges. It is a type of ion charged particle , and it's "opposite" is the anion, which is negatively-charged. Cations are attracted to anions and can form strong non-covalent bonds with them referred to as "ionic bonds" or "salt bridges.

It is a type of ion charged particle , and it's "opposite" is the cation, which is positively-charged. Anions are attracted to cations and can form strong non-covalent bonds referred to as "ionic bonds" or "salt bridges.

Sound oppositely familiar? Especially arginine. Arg has several things in common with the amino acid we looked at yesterday, Histidine His, His.

This R group might remind you of a detergent molecule. What bout Arg? Arginine also plays an important role in nitrogen metabolism. In the urea cycle, the enzyme arginase cleaves hydrolyzes the guanidinium group to yield urea and the L-amino acid ornithine.

Ornithine is lysine with one fewer methylene groups in the side chain. L-ornithine is not normally found in proteins.