Amino Acids And Function Of Protein

Different types of bonds/interactions in proteins lead to different kinds of structures. Three of the most commonly known chemical bonds in proteins include the hydrogen bond, the covalent bond, and the ionic bond. In hydrogen bonds, hydrogen interacts with oxygen, nitrogen, or fluorine to form either the alpha helix, or the beta sheet, which in turn determines its secondary, tertiary, or quaternary structure. Another type of bonds, the covalent bond, links amino acids together by sharing electrons;

The functional groups are called aminos and carboxyls. The linkage type is by using a peptide bond. The primary function of protein is build and repairs the body.

A protein has multiple existing structures, these are the primary, secondary, tertiary and quaternary structures which occur progressively. A protein is essentially a sequence of amino acids which are bonded adjacently, and interact with one another in various ways depending on the R group that the amino acid contains. There are 20 different amino acids which are able to be arranged in any given order, thus giving rise to a potential 2.433x1018 (4.s.f) different combinations, and therefore interactions between the various amino acids.

Proteins are complex structures made up of chains of amino acids. Each protein has a different function such as enzymes to catalyze reactions or protein hormones to trigger certain functions of a cell. First let’s start with the most basic component of a protein: an amino acid. An amino acid is made up of a central carbon atom attached to a hydrogen atom, a carboxyl group, an amino group, and an R group which varies

Amino Acids are essential nutrients that are the primary building blocks of proteins found in meat, dairy products, and legumes. Proteins make up 20 percent of the human body, and the amino acids that make up these proteins play a critical

The amino acids bond together in bonds called peptide bonds. A chain of amino acids is called a polypeptide chain. The structure in which the amino acids are bonded determines the function of the protein. There are about twenty different amino acids, but there is a wide variety of possible combinations that amino acids can bond, therefore proteins have quite a lot of functions. Some things proteins are used for are the building of the muscles, tendons, organs, glands, nails, and hair. There are many more different functions for proteins. To detect proteins in test materials, there is an identifying agent called Biuret Solution which when mixed with the test material. It turns purple if it contains a protein. The darker the violet color, the more concentrated it is with protein.

They are made up of amino acids (consists of amino group, carboxyl group, hydrogen atom, and R group). Polypeptide bonds form between amino acids to form polypeptide chains. Amino acid sequence is primary protein structure. The secondary structure is the bonding pattern of the amino acids (e.g. helix, sheet, etc.). The tertiary structure consists of the domain, where the sheets or helixes fold on each other and become stable. The quaternary structure consists of several polypeptide chains that form advanced proteins such as human leukocyte

There are 20 amino acids. Most of the time you use an L-enantiomer of the amino acid, however, you can have D-enantiomer forms.  D-forms are often found in antimicrobial compounds and ionophores.

The structure of an enzyme as protein has a primary, secondary, tertiary, and sometimes quaternary structure. The primary structure of an enzyme, like any protein, is the order of its amino acids. The secondary structure involves alpha helices and beta pleated sheets. Alpha helices are a coil that is formed by hydrogen bonding between every fourth amino acid. Beta pleated sheets are formed by hydrogen bonding between two or more parts of the polypeptide chain that are side by side. The tertiary structure contains disulfide bridges, ionic bonds, hydrophobic interactions, and hydrogen bonds. Disulfide bridges are the result of two sulfhydryl groups interacting because the the folding of the protein. Ionic bonds can form between polar groups on amino acids. Hydrophobic interactions are the cluster of amino acids with nonpolar side chains that is commonly seen in proteins. Hydrogen bonds can also form. The quaternary structure of an enzyme is when multiple proteins are bonded together in one complex made of proteins subunits.

Proteins are biological macromolecules which consist of a chain of amino acids joined by peptide bonds, which can either be alpha-helix or beta-pleated secondary structures. Amino acids are the monomer of proteins formed of a carboxyl group and an amino group, which are coded for by DNA. Deoxyribose nucleic acid (DNA) is formed by nucleotides which form phosphodiester bonds between them and codes for protein. The DNA is transcribed by mRNA and then translated by tRNA when read in triplet anticodons, which then forms an amino acid, followed by forming proteins. This is simply background information about how proteins are formed, and what allows the monomers of it to exist.

The primary structure of a protein is simply the sequence of amino acids. The structure or

Amino acids are the smaller building blocks which protein is made of. There are 20 different amino acids. Depending on length, sequence of amino acids and function; each protein has unique different from each other. These amino acids have unique 3D shapes by fold up in complex ways.

secondary structures are held tightly together by hydrogen bonds. Hydrogen bonds between amino acid residues are especially

Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).

Proteins are one of the most important biological molecules in the body; they make up more than 50% of the dry mass in human body cells. Their simple structure can be described as amino acid polymers as they are made up of many amino acid monomers stringed together in a linear fashion, which then gives rise to more complex structures, as various bonding and manipulation takes place. The name ‘protein’ comes from the Greek word meaning ‘holding first place’ which supports the fact that they are essential to life. Proteins, depending on their structure and where they are found, play very different roles in an organism. One of the main types of proteins are enzymes which act as biological catalysts, and are fundamental to the chemical