Protein Macromolecules

Biomolecules are present in every living organism. Larger biomolecules (macromolecules) consists of proteins, lipids, and carbohydrates. In layman’s terms, proteins are long chains of amino acids that have many functions such as, providing structural support and regulating many body processes. Lipids are the scientific term used for fats. There are many different types of fats, but they all share one common characteristic: They are not soluble in water. Lipids provide protection and insulation to organs and also act as an energy source. Carbohydrates are made up of carbon, hydrogen,

Proteins are the basis of the protoplasm (fluid living content of the cell that contains the cytoplasm and cell nucleus) and are found in all living organisms. Proteins make up the bulk of animals body’s non-skeletal structure. As enzymes, they catalyze biochemical reactions; as antibodies, they prevent the effects of invading organisms; and as hormones, they control metabolic processes (C. Bissonnette, 2011). The Biuret test was used to detect the presence of peptide bonds within proteins, and they were found present in test tube #9 (control for peptide bonds).

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.

Macromolecules come in the forms of lipids, proteins, nucleic acids, and carbohydrates. These 4 types of macromolecules are in everything we eat like grains, protein, fruits and vegetables, and dairy. During the week of September 12 through September 18 I used the Super Tracker app to record my daily calorie intake. The program recorded every single food and liquid item I ate and created a graph to show how much of each food group I ate in a day. Sometimes I had more dairy than vegetables, sometimes I had more fruits than grains. Every day was different. I sometimes went over the daily limit of saturated fat or sugars. Sometimes I went under the suggested amount that I should have in a day. By recording and understanding which macromolecules I consumed in a day, I could understand how my body is functioning after certain types of macromolecules went into my system. I could also see what kinds of foods I should be eating more or less of to maintain a healthy lifestyle.

Dehydration-synthesis is a reaction that occurs to form different types of macromolecules. It is a reaction that leaves a macromolecule structure along the lines of developing its own specific function in a living organism. The 4 most common ones are carbohydrates which includes monosaccharides and polysaccharides, lipids, proteins and nucleic acids (Mack 2012). Scientists identify different types of macromolecules to achieve a better understanding on how they function in our bodies. This can be achieved by studying their chemical properties and structure.

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

is loss of its structure. This occurs when the ionics and hydrogens bonds of the protein

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

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 biological macromolecules made from smaller building units called amino acids. There are 20 natural occurring amino acids which can combine in various ways to form a polypeptide. There are four distinctive levels of protein structure: primary, secondary, tertiary and quaternary. The primary structure of a protein is important in determining the final three dimensional structure and hence the role and function of a particular protein, both in the human body and in life around us. The secondary structure of a protein can fall into two major categories; α-helices or β-sheets, other variants also exist such as β-turns {{20 Brändén, Carl-Ivar, 1934- 1991}}. The precise folding or these secondary structures into a three dimensional shape is known as the tertiary structure of a protein and multiple polypeptides bound together via covalent and non-covalent bonds forms the complex quaternary structure of a protein.

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.

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).