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Comparison of Ionic, Polar Covalent, and Nonpolar Covalent Bonds Formation of an Ionic Bond • A valance electron from Na is transferred to Cl • Cl now has 18e and 17p resulting in a – charge • Na has 10e and 11P resulting in a + charge. Nonpolar and Polar Covalent Bonds Non polar covalent Bonds equally share electrons Polar covalent bonds share electrons unequally Hydrogen Bonds • Too weak to bind atoms together – (intra-molecular bonds= within molecule) • Important as inter-molecular bonds – between to different molecules – Important for giving proteins (enzymes) and DNA both shape and functionality. • Hold water molecules together – Responsible for surface tension in water Hydrogen Bonds in Water Hydrogen Bonds Properties of Water • Water makes up to 50-80% of all living cells. • Water stabilizes internal temperature of the body – Hydrogen bonds stabilize large shifts in temperature • Evaporate cooling (sweating) is critical from maintaining 98.6 degrees temperature in hot environments or increased physical workloads. • Water is necessary for all biochemical reactions that take place in the body. Polarity of Water • Oxygen has a greater electronegativity. • Hydrogen’s one electron spend more time in Oxygen's outermost energy level. • The result is more electrons around the oxygen making it more negative. • Hydrogen losses its electron. Its proton is unopposed making it more positive. Properties of Water • Water makes up to 50-80% of all living cells. • Water stabilizes internal temperature of the body – Hydrogen bonds stabilize large shifts in temperature • Evaporate cooling (sweating) is critical for maintaining 98.6 degrees temperature in hot environments or increased physical workloads. • Water is necessary for all biochemical reactions that take place in the body. Properties of Water • Water is a powerful splitting agent. (Hydrolysis) means water splitting. Occurs in breaking down reactions • Is known as the universal solvent. ( Polarity allows it to dissolve stuff.) water molecules slit the ionic bonds in Na+Cl- Polarity • Polar molecules associate with water and will dissociate from lipids (fats) . – Polar = hydrophilic (philic = loving) – Lipophobic (lipid fearing) • Non-polar molecules associate with lipids will not associate with water and are considered to be – Non-polar = hydrophobic (water fearing) – Lipophilic= Lipid loving Organic Compounds • Organic compounds contain carbon as the backbone. • It has the ability to create 4 covalent bonds which is important for making large complex structures. • Organic compounds include : – – – – Carbohydrates (sugars) Lipids (fats and oils) Proteins ( muscle, enzymes) Nucleic acids (DNA and RNA) • They may be built up or broken down depending on what the system requires. • May have a variety of functional groups Dehydration Synthesis • • • Dehydrate( remove water)/ Synthesis( Build) Monomers bond together to form a polymer with the removal of a water molecule (dehydration) Removal OH– of one and H+ of the other hydroxyl group forms the water. – A covalent bond will result. Hydrolysis • Translates into Water/splitting • Addition of a water to a polymer causes (lysis) of the covalent bond joining the 2 monomers. – Reestablishes the hydroxyl groups in both monomers • All digestion reactions consists of hydrolysis reactions Monomers/Polymers Carbohydrates Monosaccharides Polysaccharides Fats (lipids) Glycerol + 3 fatty Acids Triglycerides Protein Amino acids Polypeptide Nucleic Acids nucleotides Dehydration Synthesis Hydrolysis DNA, RNA Carbohydrates Hydrophilic organic molecule that : contain carbon, hydrogen, and oxygen 1:2:1 atomic ratio( carbo/carbon:hydrate/H2O) – i.e. glucose = C6H12O6 • Names of carbohydrates – word root sacchar- or the suffix -ose often used • Glucose is a monosaccharide which functions as a major fuel source for the cells. Carbohydrates • Dehydration synthesis reactions allow the cell store excess carbohydrates in the form of glycogen. • Hydrolysis reactions allow the cell to break the bonds holding the polysaccharide together allowing it to release more simple sugars. Disaccharides • Major disaccharides – sucrose = table sugar • glucose + fructose – Lactose = sugar in milk • glucose + galactose – Maltose = grain products • glucose + glucose • All digested carbohydrates converted to glucose broken down in ATP (Cellular fuel). Glycogen • Glycogen is an energy storage polysaccharide produced by animals. 2 storage sites: – Liver cell: synthesize glycogen after a meal which can be broken down later to maintains blood glucose levels. – Muscle cells: Store glycogen within the muscle at is only used by the muscle cell. Starch and Cellulose • Starch: is the storage form of sugar produced by plants. We produce an enzyme that breaks the bonds between the sugars allowing digestion to occur. i.e. potatoes and grains • Cellulose: provides structure to plants but contains a different type of bond. The β form is insoluble because we don’t produce the enzyme .i.e. dietary fiber Lipids • Hydrophobic organic molecule – Composed of carbon, hydrogen and oxygen – Better fuel source since it contains many more carbon and hydrogen molecules. • There is an unlimited supply. • Chain of 4 to 24 carbon atoms – carboxyl (acid) group on one end, methyl group on the other and hydrogen bonded along the sides • Classified – saturated - carbon atoms saturated with hydrogen – unsaturated - contains C=C bonds without hydrogen Lipids Found in the Body • Neutral fats – found in subcutaneous tissue and around organs. • Phospholipids – chief component of cell membranes • Steroids – cholesterol, bile salts, vitamin D, sex hormones, and adrenal cortical hormones • Eicosanoids – prostaglandins, leukotrienes, and thromboxanes: – These play a role in various reactions in the body such as inflammation and immunity. • Lipoproteins – transport fatty acids and cholesterol in the bloodstream • Fat-soluble vitamins – A,D, E, and K Triglycerides • Functions – energy storage in adipose (fat) tissue – Fats contain 9 kcal per gram where as carbohydrates and proteins contain 4 kcal per gram. • They contain more energy rich hydrogen. – insulation • Prevent heat loss from the body – protection • Adipose tissue cushions the organs. Triglycerides (Neutral Fats) • Contain C, H, and O, but the proportion of oxygen in lipids is less than in carbohydrates 3 • Fatty acids are bonded to a glycerol molecule during dehydration synthesis. • At room temperature : Contain double bonds. – when liquid called oils • often mono and polyunsaturated fats from plants – when solid called fat • saturated fats from animals. – No double bonds. • Function - energy storage, insulation and shock absorption Neutral Fats (Triglycerides) • Composed of three fatty acids bonded to a glycerol molecule Phospholipids • Modified triglycerides with two fatty acid groups and a phosphorus group Protein Functions – Catalysts • proteins which are enzymes significantly increase the rate of a chemical reaction i.e. Salivary Amylase increases the rate of hydrolysis of starch. – Structural • hold the parts of the body together i.e. collagen, elastin and keratin – Communication • act as chemical messengers between body areas .i.e. hormones such as insulin. – Transport • allow substances to enter/exit cells • Carry things in the blood i.e. hemoglobin, lipoproteins, Protein Functions – Movement • Actin and myosin function in muscle contraction – Defense • Antibodies( immunoglobulins) recognize and inactivate foreign invaders( bacteria, toxins, and some viruses) – Metabolism • Help regulate metabolic activities, growth and development – Regulation of pH • Plasma proteins such as albumin can function both as an acid or a base. Therefore have an important role as a buffer Amino Acids Structure • Building blocks of protein • Amino and carboxyl group groups are common in all Amino acids. • R-group (radical group): 20 amino acids are different both structurally and from a functional level. Different R- groups Protein • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds • Animal ,dairy and right combination of beans and rice are good sources of protein. • Enzymes are specific types to proteins that enable reactions. Protein Structure • Primary structure – amino acid linked together by peptide bonds. The order of the amino acids critical for both form and function. No hydrogen bonds formed. • Secondary structure :The primary structure will now form hydrogen bonds and take one of 2 forms: – α helix (coiled), β-pleated sheet (folded) • Tertiary structure – more hydrogen bonds form and increased interaction between R groups in surrounding water results in protein taking a globular 3 dimensional shape. • Quaternary structure – two or more separate polypeptide chains conjugate and form a functional protein • Hemoglobin. Structural Levels of Proteins • Primary – amino acid sequence • Secondary – alpha helices or beta pleated sheets Structural Levels of Proteins • Tertiary – superimposed folding of secondary structures – Most enzymes are in this form. • Quaternary – polypeptide chains linked together in a specific manner Functional Proteins (Enzymes) • Enzymes are chemically specific. They fit a specific substrate like a lock and key. • Enzyme names usually end in –ase – for example Lactase will be specific for the substrate lactose ( Glucose Galactose) » Gycosidic bond • Frequently named for the type of reaction they catalyze i.e. hydrolases add water during hydrolysis reactions. • lipase/lipids, protease/ proteins, • Act as biological catalysts which lower activation energy allowing reactions to occur at faster rates. Activation Energy • Activation energy refers to the extra energy required to break an existing chemical bonds and initiate a chemical reaction. – Activation energy determines rate of reaction (higher activation energy = slower reaction) – catalyst - substance that lowers the activation energy by influencing (stressing) chemical bonds Characteristics of Enzymes Enzymatic Reaction Steps Enzyme Substrate Complex • Enzymes need their 3 dimensional structure – created by both Hydrogen and disulfide bonds which is specific to a certain substrate. – Proper conditions are needed to keep these enzymes functioning. – pH – Temperature Protein Denuaturation • Hydrogen bonds are broken and tertiary level protein reverts back to primary structure. Peptide bonds are still intact. Protein Denuaturation • Proteins will become denatured if: – ∆ pH – ↑ temperature • Hydrogen bonds are broken from complex tertiary level proteins to basic primary structure. – Peptide bonds are still intact. • Visible changes you see when frying an egg Nucleic Acids • Two major classes – DNA and RNA • Composed of carbon, oxygen, hydrogen, nitrogen, and phosphorus • Five nitrogen bases contribute to nucleotide structure • Adenine (A) Thymine (T) • Guanine (G) Cytosine (C) • Uracil (U) replaces Thymine in RNA Nucleotides The structural unit of the a nucleotide is composed of • N-containing base A,T,C,G and U in RNA • Pentose sugar: Ribose, and deoxyribose • Phosphate group Deoxyribonucleic Acid (DNA) • Double-stranded helical molecule confined in the nucleus of the cell • Helical shape is a result of H-bonds between a purine on one strand and a pyramidine on the other strand – A only pairs with T – G only pairs with C • Replicates itself before the cell divides, ensuring genetic continuity • Provides instructions for protein synthesis Structure of DNA Structure of DNA Ribonucleic Acid (RNA) • • • • 1. Single-stranded molecule Made from the nucleotides that complimentary pair A U G C Three varieties of RNA: messenger RNA: transcribe DNA and carry it out of nucleus. 2. transfer RNA: Bring amino acids to site of protein synthesis (ribosome). 3. ribosomal RNA: building blocks of ribosomes ,made in the nucleolus Adenosine Triphosphate (ATP) Adenine-containing RNA nucleotide with three phosphate groups • Second and third phosphate groups are attached by high energy covalent bonds • The 3rd high energy phosphate bond of ATP is hydrolyzed producing ADP + P + energy – The cell can recycle the ADP and P back into ATP using the energy harvested from dietary foods primarily carbohydrates and lipids. • Source of immediately usable energy for the cell. – It is the currency that all cellular reactions accept. Adenosine Triphosphate (ATP) Figure 2.22 How ATP Drives Cellular Work Figure 2.23