Tertiary Proteins Globular

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.

Creutzfeldt-Jakob Disease: It happens when a prion protein misfolds itself, thus causing a “domino effect” which unfolds itself causing a malfunction.

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.

Proteins are the metabolic workhorses of the cell; they engage in a variety of essential activities ranging from enzymatically catabolizing macromolecular food sources to serving as structural components that maintain cell stability. Maximizing protein function relies on intricate non-covalent interactions occurring on the secondary, tertiary, and quaternary levels that help determine the overall shape of the protein. In their native states, proteins will assume the most energetically favorable configuration. Occasionally however, cells are exposed to exogenous disruptions such as heat stress. Heat Stress can compromise protein three-dimensional structure. Hydrophobic residues tend to be buried in the interior of the protein but when

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.

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

The basic building blocks of proteins are amino acids, the biuret reaction tests for protein. A solution of sodium hydroxide is added to a sample then a few drops of copper sulphate solution, if positive – the solution will turn mauve. There are 20 different amino acids and they can be joined in any order. Therefore there can be many different functions. A protein consists of one or more polypeptide chains (a polypeptide chain being multiple amino acids joined together via condensation, producing a peptide bond). Different proteins have different shapes as the shapes are determined by the sequence of amino acids.

Proteins are made of amino acids, which are compounds built around a central carbon atom. Amino acids then join together through dehydration reactions. These are called peptide bonds. Many amino acids joined together are called polypeptides. A polypeptide becomes a protein when it folds into a three dimensional structure. This is the primary structure of a protein. The next structure in the hierarchy is the secondary structure. Secondary structures can either form alpha helixes, where an amino acid sequence forces the polypeptide to twist into a helical shape; or beta sheets, where an amino acid sequence forces the polypeptide into a zigzag shape. In the tertiary structure, the polypeptide folds several times on itself to form a more complex three dimensional shape. A quaternary structure is when two tertiary structures interact with each other. This is when a protein becomes a functional

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.

The two main basic secondary structures are the alpha helix and the beta sheet. The alpha helix secondary structure of the protein coils because of the hydrogen bonds between the backbones of their amino acids. The backbone of the amino acid is the peptide bonds. So because of the hydrogen bonds forming between the amine nitrogens and the carbonyl oxygens in different amino acids the protein has become a helix shape.

We know that proteins are basically just amino acids bonded by peptide bonds which form a chain. However the function of protein is determined by the structure of that protein itself, we can determine the structure of an amino acid by observing what sequence the amino are in, each protein or polypeptide as its own unique sequence of amino acids, we refer

a) The tertiary structure refers to the structural arrangement of amino acids that are found far away from one another along the polypeptide chain. The tertiary structure is overall a three dimensional shape of a protein molecule. It will bend and twist to achieve maximum stability. The shape of a tertiary structure is made when the secondary structure folds in on itself and is held in place by many bonds and interactions formed by the R groups in the amino acid chain. The bonds and interactions involved are hydrogen bonds, ionic bonds, hydrophobic interactions and disulphide bonds. These bonds and interactions are located in different areas of the tertiary structure, the hydrogen bonds are located inbetween polar R groups, ionic bonds are located between charged R groups, hydrophobic interactions are located between nonpolar R groups and disulphide bonds are formed generally in the endoplasmic reticulum by oxidation ."Hydrogen bonds may form between different side­chain groups." Hydrophobic interactions are brought about in an aqueous site. The tertiary structure is held together mainly by interactions that are located at the R groups.

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

These new formations are held together by hydrogen bonds. The third level is the tertiary structure. The tertiary structure of a protein is a contorted secondary structure being twisted and folded all out of shape to form a 3-d complex. The type of bonding that holds these formations together are weak interactions such as hydrophilic, hydrophobic, ionic, and hydrogen bonds. These bonds are individually weak, but collectively strong. The forth level, which completes a protein, is quaternary structure, which occurs when two or more tertiary structures are joined together by polypeptide bonds.