Formation Of Dipeptides And Polypeptides From Amino Acids

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;

Proteins are polymers made by joining up small molecules called amino acids. Amino acids and proteins are made mainly of the elements carbon, hydrogen, oxygen and nitrogen.

A chemical reaction involving the transfer of electrons rather than molecules is classified as a Redox reaction. A reaction involving the loss of electrons is called Oxidation, and a reaction involving the gain of electrons is called Reduction. Oxidation and Reduction always occur together, as one reactant loses electrons, and the other gains them. This exchange often effects the physical states of molecules, as their solubility is changed with their charge.

Box on right illustrates the peptide bond resulting from the condensation of both the amino acids. The box on the left illustrates the separation of the hydroxide group from glycine and the hydrogen atom from valine.

Condensation reaction is a chemical reaction that joins two reactants to form a larger molecule with the loss of a small molecule, usually water. 1 This reaction is used as a basis for many important process in the plastic/food industry. The most common being the formation of ester, also known as esterification. When a carboxylic acid is reacted with alcohol in the presence of a dehydrating agent, ester and water molecule are formed as products:

Amino acids can be used to synthesize proteins for cellular structure; for energy; and to synthesize proteins that function in various body processes.

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

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

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

This is done by means of the aminoacyl attachment site (the site at which the amino acid is attached to the tRNA molecule). Each tRNA molecule, by means of their anticodons (a sequence of three exposed free bases complimentary to that of the codons on

Amide bonds are a vital part of nature. Proteins contain peptide bonds that are positioned between amino acids and make-up the backbone of the protein structure. Also, the carbon is made a better electrophile after transfer RNA activates the carbonyl group. Amides are made when carboxylic

They are known to be the workhorses of the body cell that carries out diverse catalytic and structural roles into building the structures of all living organisms [15]. The basic structure of protein is a chain of amino acids that supplies energy to a body. There are 20 different naturally occurring amino acids that make all types of protein. Proteins come in various sizes and shapes. Some comes in a thread-like shape known as fibrous proteins and they tend to have structural or mechanical roles. Others come in spherical shapes, known as the globular proteins [16]. These spherical proteins function as enzymes, transport proteins, or antibodies. The key function of protein is based on its ability to recognize and bind specific ally to molecules, it also need to be in the right shape in other to function properly [15]. The primary structure of proteins is a linear sequence of amino acids encoded by DNA. This sequence controls how protein folds into three dimensional structure, the stability of its resulting structure [17], and functions. It is important to add that protein is an important building block of bones, skin, blood and

This assignment will outline the function of proteins in living organisms and the important roles of different types of protein. “Protein composes 10-30% of cell mass and is the basic structural material of the body” (Marieb E.N.M et al, 2004). Protein is a nutrient that living organisms need to exist and grow, as well as water being a key feature. “All protein contains carbon, oxygen, hydrogen and nitrogen” (Marieb E.N.M et al, 2004). Amino acids form links of 20, “The sequences at which they are bound together produces proteins that vary widely in both structure and function” (Marieb E.N.M et al, 2004).

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).