* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download Macromolecules Power Point File
Protein (nutrient) wikipedia , lookup
Intrinsically disordered proteins wikipedia , lookup
Circular dichroism wikipedia , lookup
List of types of proteins wikipedia , lookup
Genetic code wikipedia , lookup
Amino acid synthesis wikipedia , lookup
Protein structure prediction wikipedia , lookup
I. The Structure and Function of Macromolecules A. Macromolecule- Large molecules, some with molecular weights exceeding 100,000 Daltons 1. Macromolecules are composed of polymers. Chains of similar subunits 2. Monomers- individual subunits that make up polymers 3. Polymers and molecular Diversity a) All macromolecules are composed of 40-50 of the same monomers b) All proteins in all organisms are made of the same 20 amino acids. Just as 26 letters make all words 4. Making a Breaking Polymers a) Condensation Reaction- usually occurs between –OH groups of two monomers. H2O is removed linking the monomers with an oxygen bridge b) Hydrolysis- breaking apart polymers at their oxygen bridge by adding H2O which results in two monomers B. Carbohydrates- sugars and starches that serve as important sources of fuel and structural components Carbohydrates 1. Monosaccharides- single sugars with 3-6 carbons. (Glucose, Fructose, Galactose) 2. Disaccharides- two monosaccharides joined in a condensation reaction 3. Polysaccharides- many single sugars joined together Types of Polysaccharides a) Starch- storage form of carbohydrate in plants. (Spiraling 1-4α glycosidic bonds) b) Glycogen- Storage form of carbohydrates in animals. (Spiraling, highly branched, 14α glycosidic bonds) c) Cellulose- Structural polysaccharide in plants. (Straight polysaccharide with 1-4β glycosidic bonds) 4. Modified Carbohydrates A) Chitin- main component of the exoskeletons of arthropods. Contains a monosaccharide derivative glucosamine Lipids Animal Fat Plant Oils Waxes C. Lipids- molecules used to store energy in organisms as well as structural materials. Made of C, H, O. Less oxygen than in carbohydrates. Twice the amount of energy. Soluble in non-polar solvents 1. Neutral Fats- 1 glycerol with fatty acid chains Types of Lipids a) Saturated fat- Solid at room temperature. Many hydrogen. No double bonds between carbons. Animal fats. Cause arteriosclerosis. b) Unsaturated and Polyunsaturated FatOils. Liquid at room temperature. Double bond between some of the carbons. 2 essential fats are oleic and linoleic acid. These cannot be synthesize by the body but must be in the diet 2. Phospholipid- important constituents of the cell membrane made of a glycerol and 1-2 fatty acid chain with the glycerol bonded to a phosphate group. Contains a hydrophilic and hydrophobic end Other Lipids 3.Carotenoids- red and yellow plant pigments that play a role in photosynthesis A) splitting the orange plant pigment carotene yeilds a retinol molecule B) Retinol molecules play an important role as photoreceptors in eyes 4. Steroids- class of compounds with four interlocking rings to form many biologically important molecules (Cholesterol, bile salts, hormones etc….) D. Proteins- all enzymes, some hormones and many structural components of the cell are proteins. 1. Subunit Structure (Protein monomer = Amino Acid) a) Amino acids are composed of an amino group (-NH2) and an acidic carboxyl group but different r groups R group Amino group Carboxyl group b) The “R” group determines the identity of the amino acid Amino Acids with Hydrophobic Side Groups Note the methyl groups at the bottom of the chains Amino Acids with Hydrophilic Side Groups Note the charged or polar groups at the bottom of the chains And Some Amino Acids are in Between Hydrophobic and Hydrophilic regions influence protein shape. C) Amino acids can serve as acids or bases and are therefore considered buffers D) Amino acids are linked by a condensation reaction and form peptide bonds E) When many amino acids are joined, a polypeptide is formed 2. Levels of Protein Structure A) Primary- Linear sequence of amino acids joined by peptide bonds in a condensation reaction B) Secondary- coiling and pleating of amino acid chains (α helixes or β pleats) stabilized by hydrogen bonds C) Tertiary- overall shape caused by the folding or twisting of the secondary structure D) Quaternary Intertwining of multiple polypeptides to produce a highly specific 3D shape 3. Importance of Proteins a) Proteins are the most abundant molecule in living cells. Functionally diverse, They control all life functions Class Function Example A) Enzymes. Control Chemical Reactions. Maltase B) Structure. Building material of cells. Collegen C) Contractile. Movement. Actin and myosin D) Hormones. Regulatory chemicals. Insulin E) Transport. Ship important substances hemoglobin F) Defense Fight Disease antibodies c) Proteins are sensitive and may denature (change shape) and become non functional. Heat, pH and metals all can cause denaturation E. Nucleic Acids- large complex molecules formed of smaller smaller units called nucleotides 1. Nucleic Acid structure (monomer = nucleotide) a) Nucleotide consists of a sugar a phosphate group and a nitrogen base b) Sugars: 1) Ribose in RNA 2) Deoxyribose in DNA c) Bases: 1) Purines (2 rings) Adenine and Guanine 2) Pyrimidines (1 ring) cytosine and Thymine Nucleic Acids 2. DNA structure is a double helix with the base pairing of Thymine & Adenine and Cytosine & Guanine. 3. RNA structure is a single spiral with Uracil replacing thymine. 4. Nucleic Acid Function a) DNA carries the genetic code. The information for constructing proteins b) RNA Carries the genetic code to the ribosome. c) Adenosine Triphosphate (ATP) supplies energy to the cell d) Other Nucleotides and dinucleotides are electron transport molecules and energy carriers – GTP, UTP, CTP – dGTP, dATP, dCTP, dTTP – AMP, NAD+, NADP, FAD