Proteins

The basic monomer for proteins is amino acid.

These molecules are called substrates.

Intrinsic proteins are the integral proteins inside the plasma membrane, or phospholipid bilayer, of a cell. The reason they are called intrinsic is because they cannot be released unless the membrane is disrupted.

A protein is driven into its structure

by hydrophobic interactions with water. The final folding

of a protein is determined by its primary structure-by the

chemical nature of its side groups. Many proteins can be

fully unfolded ("denatured") and will spontaneously refold

back into their characteristic shape.

The stability of a protein, once it has folded into its 3-D

shape, is strongly influenced by how well its interior fits

together. When two nonpolar chains in the interior are in

very close proximity, they experience a form of molecular

attraction called van der Waal's forces. Individually quite

weak, these forces can add up to a strong attraction when

many of them come into play, like the combined strength

of hundreds of hooks and loops on a strip of Velcro. They

are effective forces only over short distances, however;

there are no "holes" or cavities in the interior of proteins.

That is why there are so many different nonpolar amino

acids (alanine, valine, leucine, isoleucine). Each has a different

sized R group, allowing very precise fitting of nonpolar

chains within the protein interior. That's

why a mutation that converts one nonpolar amino

acid within the protein interior (alanine) into another

(leucine) very often disrupts the protein's stability; leucine

is a lot bigger than alanine and disrupts the precise way the

chains fit together within the protein interior. A change in

even a single amino acid can have profound effects on protein

shape and can result in loss or altered function of the

protein.

The sequence of the bases on DNA is copied as a sequence of bases on RNA (messenger RNA). This is finally translatedinto a sequence of amino acids in the protein which determines the protein's structure and function.

The gallbladder, which is an accessory organ of the small intestines, makes bile which is secreted into the small intestine and emulsifies (breaks down) fats.

Golgi complex or Golgi apparatus, or something like that.

well with out protein you will be as week as a cat but not only protein makes you strong, you need carbohydrates to make your protein work.

You might be thinking specifically about Pepsin. This enzyme is in the stomach and it digests proteins into peptides.

Source: Wikipedia!

No, trypsinogen is a zymogen, an enzyme precursor, an inactive chemical produced by the pancreas. In the intestine, trypsinogen is activated by the mucosal enzyme enteropeptidease to produce the enzyme trypsin which is critical to digestion.

Proteins have primary structure, which is their amino acid sequence, secondary structure, which is either the alpha helix or the beta pleated sheet, tertiary structure, the protein's geometric shape, and quaternary structure, the arrangement of multiple protein subunits.

Proteins are made up of amino acids, which are known as the building blocks of proteins. There are 20 different types of amino acids that can combine in various sequences to form different proteins with diverse functions.

Ribosomes are the structure that synthesize proteins. They are located on the endoplasmic reticulum, which is an organelle inside the cell.

To answer this question we have to talk a process called: "Translation". After the "Transcription", that is, the mechanism from where a mRNA molecule is synthesized from a DNA double helix. The mRNA molecule migrates outside the nucleus to the cytoplasm and specifically to the ribosomes (a complex protein organelles that serve as building machines for new polypeptide molecules). The mRNA molecule carries the specific sequence for the synthesis of the new polypeptide (protein) chain and serves as a "template" for the proper order of the amino acids that will constitute the new protein molecule. To add the amino acids to the growing polypeptide chain are necessary the tRNA molecules (these RNA structures carry a single amino acid that will be added to the growing polypeptide chain). Each tRNA has a specific three-nucleotide sequence (called "anticodon") that recognizes the corresponding three-nucleotide sequence (codon) on the mRNA molecule. Each amino acid monomer (carried by its particular tRNA) is anchored, one by one, to the previous amino acid that was added before by a peptide bond. This mechanism is taken place in a particular region of the ribosome, a cleft that provides the nascent polypeptide's exit path.

It is the ribosome. Proteins are synthesized on that

Compliment proteins are proteins found in the blood that fight off infections and diseases. They are produced by predecessor proteins, and are called "compliment" proteins because they participate in a compliment reaction.

No, they are called phospholipids because they are made of lipids and phosphate group. Most phospholipids contain a diglyceride, a phosphate group, and a simple organic molecule such as choline.

In addition to providing structural support, actin filaments are involved in movement when they interact with the specialized protein myosin. Myosin is a motor protein that converts the chemical energy in ATP into the mechanical work of movement. The interaction between actin and myosin that produces movement: When ATP binds to themyosin and is then hydrolyzed to ADP, the "head" region of the myosin molecule binds to the actin filament on the slide. The movement of this protein causes the ctin filament to slide. This type of movement is analogous to a line of people who are passing along a long log or pole, the people are myosin molecules; the log is the is the actin.

Lets look at two examples of a lipid in a cell.

# Phospholipid: A phospholipid chain(composed of a glycerol and 3 fatty acid) is an essential part of the cell membrane. # cholesterol: Cholesterol controls the fluidity of the cell membrane.

Protein is needed by the body for many of its different functions. The muscles, organs, bones, and immune system all require protein to work properly. You get protein by eating foods like red meat, eggs, and diary products.

In a cell, ribosomes make proteins with amino acids based on the RNA blueprints copied from the DNA.

the endoplasmic reticulum prepares protien. by saira

Yes; during translation.

1. Enzymes: Catalyze biochemical reactions
2. Structural proteins: Provide support and strength to cells and tissues
3. Transport proteins: Facilitate the movement of molecules across cell membranes
4. Hormones: Regulatory proteins that coordinate various physiological processes.

Chloroplasts for photosynthesis, (plants)

Human protein synthesis is Mitochondria for energy (human)