Protein Questions!?

Question

what are monomers of them. what are they in the body and what are they used for? what elements are they made of?

and the tough one for all you bio majors lol..

HOw many possible combinations of proteins are possible with 20 different amino acids?

Thanks!! 10 pts to Best answer..

Answer 1

Proteins are biomolecules formed by the bonding of monomers called "aminoacids".

Aminoacids are joined together by peptidic bonding (which is an amide bonding: -COONH-)

In general, aminoacids are formed by the following elements:

Carbon
Oxygen
Hydrogen
Nitrogen
Sulphur (just in a couple of aminoacids cystin and cystein)

Proteins have the following functions in the body:

a) Structural.- For example in forming tissues as muscular tissue, cartilaginous tissue.

b) Catalytic.- In the form of enzymes. Enzymes are proteins with catalytic activity and they are fundamental in metabolism of all living creatures.

c) Energy source.- In extreme cases of bad nourishment body can take proteins as a food of energy metabolizing them in specific biochemical pathways. Energy yieldings in this case are lower than glucides and lipids.

Knowing that proteins are made from 20 or more joined aminoacids, you can imagine that there are trillions of possible combinations (Insulin for example is composed by 51 aminoacids, so, if you could build another proteins with that same number of units, you should array 20 aminoacids in 51 places with ot without repetition, so the number of combinations could be 20^51 = 2.2517 x 10^66 A lot of arrays!!).

Good luck!

Answer 2

1. The monomers (or building blocks) are the 20 amino acids.
2. Some proteins are structural parts of hair, fingernails, membranes, etc. Proteins carry oxygen and provide immunity, among other functions. Some proteins are enzymes that catalyze reactions in the bdy.
3. Proteins are made of C, H, O, N, and S.
4. Endless kinds of proteins can be made from the 20 amino acids since they can be arranged in any order and the proteins can be very large molecules.

Answer 3

Take your weight in pounds and multiply by 0.36 to get the number of protein grams you need daily. There is a healthy margin of error built into this calculation, so you can get by on even less. You don't need to get lots of protein from other stuff. As a meat eater, you were likely getting 2-4 times the protein you needed every day, which is actually detrimental to your health. Excess protein leaches calcium from the bones, irritates the immune system and overburdens the kidneys. If you're eating poultry and seafood (and presumably dairy and eggs, too) you're probably still getting more than you need. Even vegetarians tend to get extra, just not to the extent that meat eaters do. It's a complete myth that plant foods are deficient in protein. Many plant foods, on a per calorie basis fare much better than even beef. Vegans can easily get enough protein from soybeans and soy foods (tofu, tempeh, edamame, tvp, faux meats,) beans and other legumes (lentils, peas, peanut butter, chickpeas,) whole grains, nuts, seeds, vegetables (especially dark green ones,) and mushrooms. If we can get plenty, anyone adding animal foods on top of that can too.

Answer 4

The monomer of proteins is amino acid.They come in the form of enzymes,hormones,keratin,etc.

1.Enzymes
Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions. In these reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products. Almost all processes in the cell need enzymes in order to occur at significant rates. Since enzymes are extremely selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.

Like all catalysts, enzymes work by lowering the activation energy (ΔG‡) for a reaction, thus dramatically accelerating the rate of the reaction. Most enzyme reaction rates are millions of times faster than those of comparable uncatalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more specific. Enzymes are known to catalyze about 4,000 biochemical reactions.[1] Not all biochemical catalysts are proteins, since some RNA molecules called ribozymes also catalyze reactions.

Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, pH, and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew).

2.Hormones
A hormone is a chemical messenger from one cell (or group of cells) to another. All multicellular organisms produce hormones (including plants - see phytohormone).

The best-known animal hormones are those produced by endocrine glands of vertebrate animals, but hormones are produced!!!!!!!@#$%^ by nearly every organ system and tissue type in an animal body. Hormone molecules are secreted (released) directly into the bloodstream; some hormones, called ectohormones, are not secreted into the blood stream, they move by circulation or diffusion to their target cells, which may be nearby cells (paracrine action) in the same tissue or cells of a distant organ of the body. The function of hormones is to serve as a signal to the target cells; the action of hormones is determined by the pattern of secretion and the signal transduction of the receiving tissue.

Most hormones signal a cell change by combining with a receptor. For many hormones, including most protein hormones, the receptor is embedded in the membrane on the surface of the cell. The interaction of the hormone and the receptor typically triggers a cascade of secondary effects within the cytoplasm of the cell!!!!!!!!!!!!!!!!!!!!!!!!!!!, often involving phosphorylation or dephosphorylation of proteins, changes in ion channels, or increased amounts of an intracellular molecule that serves as a second messenger (e.g., cyclic AMP). The second common type of mechanism, typically involving smaller-sized hormones such as steroid or thyroid hormones, begins with entry of the hormone molecule into the cytoplasm of the cell where it combines with a loose and mobile receptor. The combined hormone-receptor ligand then moves across the nuclear membrane into the nucleus of the cell and binds to the DNA, effectively amplifying or suppressing the action of certain genes, thereby affecting protein synthesis.

Hormone effects vary widely, but can include stimulation or inhibition of growth, induction or suppression of apoptosis (programmed cell death), activation or inhibition of the immune system, regulating metabolism and preparation for a new activity (e.g., fighting, fleeing, mating) or phase of life (e.g., puberty, caring for offspring, menopause). In many cases, one hormone may regulate the production and release of other hormones. Many of the responses to hormone signals can be described as serving to regulate metabolic activity of an organ or tissue. Hormones also control the reproductive cycle of virtually all multicellular organisms.


3.Keratin
Keratins are a family of fibrous structural proteins; tough and insoluble, they form the hard but nonmineralized structures found in reptiles, birds, amphibians and mammals. They are rivaled in biological toughness only by chitin.

There are various types of keratins, even within a single animal.
Keratins are the main constituent of structures that grow from the skin:

the α-keratins in the hair (including wool), horns, nails, claws and hooves of mammals
the harder β-keratins in the scales and claws of reptiles, their shells (chelonians, such as tortoise, turtle, terrapin), and in the feathers, beaks, and claws of birds. (These keratins are formed primarily in beta sheets. However, beta sheets are also found in α-keratins.)[1]
The baleen plates of filter-feeding whales are made of them.

They can be integrated in the chitinophosphatic material that makes up the shell and setae in many brachiopods.

Keratins are also found in the gastrointestinal tracts of many animals, including roundworms (who also have an outer layer made of keratin).

Although it is now difficult to be certain, the scales, claws, some protective armour and the beaks of dinosaurs would, almost certainly, have been composed of a type of keratin.

In Crossopterygian fish, the outer layer of cosmoid scales was keratin.


4.Antibodies
An antibody or immunoglobulin is a large Y-shaped protein used by the immune system to identify and neutralize foreign objects like bacteria and viruses. Each antibody recognizes a specific antigen unique to its target.[1] This is because the two tips of the "Y" of the antibody contain a paratope (a structure analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to precisely bind together. This precise binding mechanism allows an antibody to tag a microbe or an infected cell for attack by other parts of the immune system, or to directly neutralize its target (i.e. by blocking a part of a microbe that is essential for its invasion and survival). The production of antibodies is the main function of the humoral immune system.[2]

Antibodies are soluble glycoproteins of the immunoglobulin superfamily.[3] The terms antibody and immunoglobulin are often used interchangeably. When attached to the surface of the B cell, the membrane-bound form of the immunoglobulin is sometimes referred to as the B cell receptor (BCR). Soluble antibodies are found in the blood and tissue fluids, as well as many secretions. In structure, they are globulins (in the γ-region of protein electrophoresis). They are synthesized and secreted by plasma cells that are derived from the B cells of the immune system.[4] Membrane-bound immunoglobulins are only found on the surface of B cells and facilitate the activation of these cells following binding of their specific antigen, and their subsequent differentiation into plasma cells for antibody generation, or memory cells that will remember the foreign antigen during future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding.



5.Collagen
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 25% of the total protein content.
It is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins such as enzymes; tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside certain cells. Collagen has great tensile strength, and is the main component of cartilage, ligaments, tendons, bone and teeth. Along with soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. It strengthens blood vessels and plays a role in tissue development. It is present in the cornea and lens of the eye in crystalline form. It is also used in cosmetic surgery and burns surgery.


20100 possible combinations of proteins are possible from 20 different amino acids