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What is the substrate of carboxypeptidase?
The substrate of carboxypeptidase is a peptide or protein molecule with a terminal amino acid that contains a free carboxyl group. Carboxypeptidase cleaves this terminal amino acid from the substrate by hydrolyzing the peptide bond.
What fluid in the body has the highest hydrogen ion concentration?
The fluid in the body with the highest hydrogen ion concentration is typically the stomach acid (gastric acid) due to the presence of hydrochloric acid. This highly acidic environment aids in digestion and helps to kill ingested pathogens.
Why do serum protein molecules such as albumin and lysozyme adopt different charges within the physiological pH?
Proteins are molecules consisting of a linked chain of subunits called amino acids. Twenty different amino acids occur naturally. Different proteins (arising from different genes) will have different amino acid sequences. Each amino acid has a portion called a "side chain" that is unique in chemical composition and properties. The side chain can extend into the aqueous medium surrounding the protein. Some amino acids (glutamate, aspartate) have acidic side chains and so give up a H+ ion at physiological pH and leave the side chain with a "-" charge. Other amino acids (such as arginine and lysine) have basic side chains that tend to take up a H+ ion from the surrounding water and this confers a "+" charge on these units. Some amino acids (glycine, serine) do not interact with H+ ions at all. Thus, the net charge (sum of + and - charges) on any protein at a given pH is strictly a function of its amino acid composition. The pH that causes the net charge to be zero is called the isoelectric point and this parameter is measurable in the laboratory and can vary widely among different proteins.
What is a small molecule that is linked chemically to other amino acids to form proteins?
Amino acids are small molecules that are linked together through peptide bonds to form proteins. Each amino acid has a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a side chain. The side chain determines the unique properties of each amino acid.
What is the charge of a Peptide with sequence aggdrleeq at pH 7.0?
At a neutral pH i.e. pH 7, only five of the twenty common amino acids carry a net positive or a net negative charge. Aspartic acid and Glutamic acid are negatively charged (-1), at a neutral pH the carboxlic side chains lose a H+ ion Lysine, Arginine and Histidine are positively charged (+1), at a neutral pH the side chains accept a H+ ion. All other amino acids are generally uncharged (0). It is therefore easy to work out the net charge of any sequence. All sequences contain the one letter abbreviation for each amino acid. Here the sequence is "aggdrleeq" a=alanine (uncharged = 0) g=glycine (uncharged = 0) g=glycine (uncharged = 0) d=aspartic acid (negatively charged = -1) r=arginine (positively charged = +1) l=leucine (uncharged = 0) e=glutamic acid (charged = -1) e=glutamic acid (charged = -1) q=glutamine (uncharged = 0) Add up all the charges -3, +1 gives a total peptide charge of -2.
What part of ion is part of amino acid?
The ionizable part of an amino acid is the amino group, which contains a nitrogen atom with a lone pair of electrons that can act as a proton acceptor or donor. This part of the amino acid molecule can gain or lose a proton, giving it the ability to exist in different ionic forms at different pH levels.
What ion is in every acid?
H+
This ion is in every acid is?
You're probably looking for hydrogen ion (H+).
How do you know if an amino is acidic?
An amino acid is acidic if it has a side chain that can donate a hydrogen ion (proton) in a chemical reaction. Amino acids with acidic side chains include aspartic acid and glutamic acid. The overall charge of the amino acid depends on the pH of the environment.
What happens to each of the functional groups on an amino acid when the amino acid becomes an ion?
When an amino acid becomes an ion (by gaining or losing a proton), the amino group (NH2) becomes NH3+, the carboxyl group (COOH) becomes COO-, and any side chain functional groups may be affected depending on their specific properties. The net charge of the amino acid will depend on the balance of protons gained or lost.
What is the substrate of carboxypeptidase?
The substrate of carboxypeptidase is a peptide or protein molecule with a terminal amino acid that contains a free carboxyl group. Carboxypeptidase cleaves this terminal amino acid from the substrate by hydrolyzing the peptide bond.
What ion is part of every base?
The hydroxide ion (OH-) is part of every base. It accepts protons (H+) in solution to produce water.
Why can phosphorus-32 be used to detect the presence of nucleic acids but not amino acids?
amino acids only contain carbon,hydrogen,oxygen and nitrogen. they do not contain phosphorus and cannot be incorporated. the ion phosphoric acid is found in nucleic acid.
What ion is sometimes used as a second messenger of amino acid based hormones?
Calcium ion (Ca2+) is commonly used as a second messenger of amino acid-based hormones in signal transduction pathways. It can regulate various cellular processes by binding to and activating downstream effectors such as protein kinases and phosphatases.
What ions do you see in nearly every acid and base?
Acids produce the H+ ion, and bases produce the OH- ion.
The reactions of aniline with acetic acid?
Aniline reacts with acetic acid to form anilinium acetate salt. The amino group in aniline reacts with the acetic acid to form anilinium ion, and the acetate ion is the conjugate base of acetic acid. This reaction is an acid-base reaction resulting in the formation of a salt.
Is NH2 an acid?
No, substances containing the -NH2 group are basic. The NH2- ion is extremely basic.
