Biochemistry

You mean "why is a protein least soluble when the pH of aqueous media matches the value of its isoelectric point?".

The answer is that at its isoelectric point the protein surface carries no net charge. As protein solubility is based upon favourable electrostatic interactions between the charges (negative or positive) on the protein surface and the delta-negative or delta-positive dipoles on water molecules, when there is LEAST charge on the protein surface you can also expect their to be the least favourable interactions between water molecules and the protein. As the protein-water interaction is in competition with protein-protein interactions, being at the pI most favours protein-protein interactions, which leads to precipitation, compared to protein-water interaction which lead to solvation.

Isoelectric. "equal electric [charge]"

The previous answer is incorrect in multiple ways and correct in some. It states "protein solubility is based upon electrostatic interactions between the charges (negative or positive) on the protein surface and the ...dipoles of water". Firstly, there cannot exist an electrostatic interaction (coulombic) with one charged molecule and an uncharged water molecule/induced dipole. An electrostatic force of a charged particle must have an electrolyte in solution for interaction.

What the explanation aimed to describe is the decreased ion-induced dipole forces from a charged amino acid side chain to molecules of water at the pI of the protein. The singular force of which is stronger than H-bonding (and much stronger than van der waals, london/dispersion forces). Collectively H-bonding of the exterior amino acids is a much stronger force than total of the ion-induced dipoles.

...However, if we were talking about "solvation" of the molecule, then his answer would be completely correct where at the isoelectric point the least solvation would occur, largely due to the absence of charged outer residues...

Why is the solubility not dependent on ion-induced dipole? We only have 5 natural occurring amino acid R groups that can be charged around neutral pH: aspartate, glutamate - whose side chains behave as any other organic acid in the physiological range, reacting with other amine side chains, going through esterification with alcohols, chelation of divalent metal ions, etc.

The basic residues - lysine and arginine, lysine will undergo a number of reactions with or without a protonated nitrogen. Arginine however is likely going to carry a net charge at any protein pI and is the least reactive A.A. (however its' frequency in proteins is 5.7%, of this percent a fraction of which will go toward ion-dipole surface interaction with water. The same goes for histidine but it is even less frequent in proteins (2.2%).

The pI of most any protein will be nearer to the physiological range than to either extreme, so we can rule out mass protonation/deprotonation of side chains at its pI, which is the only way ion-induced dipole forces would participate in such solubility changes anyhow.

So what does make a protein soluble/insoluble in water?

A protein's 'solubility' comes first from the specific volume of water being much smaller than the specific volume of the protein. Meaning although our protein may be more dense than water, it has a tendency to be suspended in solution because of the much larger volume occupied (this of course is not true for many types of proteins, seen more in globular proteins but the theory is the same).

The major factor of protein solubility according to pI is hydrophilic residues (vs hydrophobic) on the exterior. As the pH of the solution nears an equilibrium of oxidation/reduction of the hydrophobic exterior residues, less water molecules are forming h-bonds, dipoles, van der waals, etc on the protein's exterior. You could imagine the H2O 'dispersing' away from the membrane, decreasing the volume occupied by H2O molecules near the protein exterior. This action allows the protein to 'fall' from solution and form a precipitate at the pI of the solution. The physical chemistry behind this action is much more involved, but this should give some idea of the biochemistry of the event.

Enzymes are typically recycled in living systems by being released from their substrate and remaining unchanged after catalyzing a reaction. They can then go on to catalyze more reactions. In some cases, enzymes may be modified or degraded after use and their components reused to make new enzymes.

No, mitochondria have their own DNA separate from the nuclear DNA found in the cell. This DNA encodes for some of the proteins needed for mitochondrial function. Chloroplasts also have their own DNA, containing genes that code for some chloroplast-specific proteins.

Yes, sugar beet is a carbohydrate because it contains sugars like sucrose and fructose that are classified as carbohydrates. Sugar beets are a rich source of carbohydrates and are commonly processed to extract sugar for consumption.

the full form of DNA is dirhibonucleicacid, it is called so due to the pattern it forms, it comes into one person by inheriting their parents DNA samples, sorry its a bit difficult for me 2 make it complex but i think its good enough to work?

Tissues are integrated groups of cells that have a common function and/or structure. They are organized into specific layers or patterns to carry out specialized functions within an organism. Examples include muscle tissue for movement, nervous tissue for communication, and epithelial tissue for protection and absorption.

Yes, xanthan gum is a carbohydrate, but it is not a source of digestible carbohydrates. It is a complex sugar derived from the fermentation of corn sugars.

The crystalline derivative of amino acid cysteine is N-acetyl-L-cysteine, commonly known as NAC. This compound is a precursor to the antioxidant glutathione and is used in supplements for its antioxidant and mucolytic properties.

depends on the organism. ill assume you mean eukaryotes, since prokaryotes ("bacteria") do not really have subcellular compartments, to the classical thinking is they are kind of like a big bag with only one "place" : inside (although this is rapidly changing , with the idea the even in proks, there are special regio of hte thcell where certain thing happen...)

anyway, in euks many (glycolisis, much of anabolism) occur in the cytoplasm, with some occurring in the mitochondria (TCA, b-Ox). Various other reactions occur in other compartments (e.g Calvin cycle in choloplasts)

on the other hand you may mean where in an organism do they occur? in humans, many common rxns occur in almost all cells, but others are specialized inand occur only in some types of cells (red blood cells, adipose tissue, the liver, muscel..)

Hemoglobin levels, hematocrit levels, and red blood cell count are blood measurements that can provide information on a possible anemic condition. Anemia is often characterized by low levels of these parameters.

There are approximately 8 grams of carbohydrates in 100 ml of soy sauce.

Monosaccharides are made of a single sugar molecule, consisting of carbon, hydrogen, and oxygen atoms. They are the simplest form of carbohydrates and serve as the building blocks for more complex sugars and carbohydrates. Examples of monosaccharides include glucose, fructose, and galactose.

Souring milk causes a chemical change because it changes its state of matter (from a liquid to a semi-solid), and it grows bacteria. When milk sours it causes a permanent change, therefore making it a chemical change.

probabaly the most important reason is it is a major part of all nucleic acids, such as DNA and RNA. it is also involved in various metabolic processes and regulatory processes, and other things specific to the type of organism (i.e. bones, teeth)

The four most common elements in living things are carbon, hydrogen, oxygen, and nitrogen. These elements are essential for building organic molecules like carbohydrates, lipids, proteins, and nucleic acids that make up living organisms.

Chitin is insoluble in most solvents, including water. However, it can be dissolved in specific solvents, such as concentrated acid solutions or ionic liquids, through chemical modifications or treatments.

Yes, freezing an enzyme can affect its activity by denaturing it and changing its structure. Ice crystals can form and disrupt the enzyme's fragile structure, diminishing its function once thawed. It's best to store enzymes at their recommended temperature to maintain their stability and activity.

We can reduce it by using different antibiotics, by using them less often and fight the illness in a different maybe natural way and finally by taking the whole course of the antibiotics instead of just taking them until you feel better.

Denatured refers to when a protein loses its structure to become something akin to an amorphous blob. To really understand this though you must understand the structures of protein.

A protein is a long string or chain composed of amino acids all linked together. When proteins are formed by the body they must 'fold' themselves into a structure that is capable of work or doing a task. Once in this folded form the protein can go on to serve whatever function it serves.

Denaturing causes the protein to lose this shape and ultimately functionality. For the most part denatured proteins can be 're'natured by reversing the cause of denaturing. A familiar example of denaturing while is non reversible is cooking eggs. The egg white is rich in proteins and when heated causes the protein to lose it's form and harden. As stated this can't be reversed.

As explained above one way to denature a protein is by applying heat but also by any temperature change, pH change or even change in solvent (using formaldehyde or ethanol instead of water).

Yes, both wheat and lentils are carbohydrate-rich foods. Wheat is a starchy carbohydrate, while lentils are a good source of both carbohydrates and protein.

No, fermentation does not involve an electron transport chain. Instead, it is a metabolic process that generates ATP without the use of oxygen by using an organic molecule as the final electron acceptor.

No, chitin is a natural biopolymer classified as an organic compound. It is a structural polysaccharide found in the exoskeletons of arthropods, such as insects and crustaceans, as well as in the cell walls of fungi.

Proteins play an important role in the lifespan and quality of human life. Depending upon the roles and bonds and the structure of amino acid, the proteins in the cell membrane play the role of channels to facilitate diffusion. The resultant active transport comes due to globular proteins. These proteins have polar side groups that improve their solubility in water. The non-polar folding enables the protein strains to keep water out and this avoids unfolding. Proteins facilitate diffusion and act as transporters. They bind with glucose molecules to transport them to the other side of the membrane. This facilitates the glucose to detach. Proteins, in living organisms, play the role of channels to transfer molecules according to electrical and chemical qualities.

Proteins also function as organic catalysts in the human anatomy. They are responsible for catalyzing a number of important biochemical reactions. Proteins go beyond the body; they also affect the world at large in this capacity. The proteins, due to their tertiary structure, influence the nature of enzymes. They affect the ability of the enzymes to use energy from a reaction to affect and help one involving them. The human DNA tells of many protein rich tales! Proteins also influence the human immune system. The special immuno-proteins are blood proteins. As immuno-proteins they affect the human immune system. There are soluble proteins that get linked to antigen and affect the regulation of the immune system. They also affect hypersensitivity. The result is an attack on microbes, which helps to ward off infection.