Presentation on theme: "1Macromolecules. Molecules of Life Macromolecules organic molecules which are carbon-basedMacromolecules are large organic molecules which are carbon-based."— Presentation transcript:
Molecules of Life Macromolecules organic molecules which are carbon-basedMacromolecules are large organic molecules which are carbon-based 4 Types: –Carbohydrates –Proteins –Nucleic Acids –Lipids Carbon can form covalent bonds with as many as 4 other atoms.
Polymers MONOMERS –Molecules made from repeating units of similar compounds called MONOMERS –linked together by a series of covalent bonds. –Macromolecules are POLYMERS.
Monomers of Macromolecules
Dehydration Synthesis polymersmonomers “removing water”Forms polymers by combining monomers by “removing water”.
Hydrolysis Reaction monomers“adding water”Separates monomers by “adding water”
Chemical Reactions Hydrolysis Rxn –Bonds broken –Energy Released –Exergonic –Catabolic Dehydration Synthesis –Bonds formed –Energy Stored –Endergonic –Anabolic
Let’s Review!!! A B
How Are Macromolecules Formed? Release Energy or Store Energy? Endergonic or Exergonic? Catabolic or Anabolic?
How are Macromolecules separated or digested? Release Energy or Store Energy? Endergonic or Exergonic? Catabolic or Anabolic?
Carbohydrates General Function: –Energy storage Starch (Plants) Glycogen (Liver) –Structural Support Cellulose (Plant Cell Wall)
Carbohydrates Compounds composed of carbon, hydrogen, and oxygenCompounds composed of carbon, hydrogen, and oxygen –C(1):H(2):O(1) ratio C 6 H 12 O 6 glucose --saccharides –Monosaccharide –Disaccharide –Polysaccharide
Carbohydrate Function Polysaccharide: many sugar units
Anatomy Application Why Carb Load? Glycogen stored primarily in liver and skeletal muscles.
Lipids not soluble in waterGeneral term for compounds which are not soluble in water. –NonPolar/Hydrophobic Examples:Examples: –Fats –Oils –Waxes –Phospholipids –Steroid & Cholesterol –Triglyceride
Fat storage for energy
Building Blocks of Lipids Fatty Acids –Saturated or Unsaturated Glycerol TRIGLYCERIDE
Phospholipids Responsible for the structure and function of the cell membrane. dex.htmlhttp://telstar.ote.cmu.edu/biology/downloads/membranes/in dex.html Where do we find these?
Steroids Class of lipids characterized by a carbon skeleton consisting of four fused rings
Saturated vs Unsaturated SATURATEDUNSATURATED (cis)UNSATURATED (trans) COMPLETELY FULL OF HYDROGEN NOT FULL OF HYDROGENCHEM. PROCESS TO ADD IN MORE HYDROGEN “HYDROGENATED” ALL SINGLE BONDS IN F.ADOUBLE BONDS IN F.A. STRAIGHT TAILBENT TAILSTRAIGHT TAIL DENSLEY PACKED TAILLESS DENSLY PACKED TAILDENSE PACKED SOLID AT ROOM TEMPLIQUID AT ROOM TEMPSEMI-SOLID AT ROOM TEMP EX: BUTTEREX: OLIVE OILEX: CRISCO
Hydrogenated things What have you heard about hydrogenated and/or partially hydrogenated things? Why so bad? Can be bad: not easily broken down. Accumulates in your body tissue and arteries Trans fat video
Proteins FUNCTION Enzymes Defense Transportation Support Motion Hormones storage
Proteins Monomer of Protein = Amino Acid Polymer of Protein = polypeptide
Proteins (Polypeptides) Building Blocks: AMINO ACIDS –20 different Amino Acids –Same structure except for R group Amino Acids –Carboxylic Acid Group –Amino Group –R group (variable) –Central Carbon Amino Group Carboxylic Acid Group
Effect of different R groups: Nonpolar amino acids Why are these nonpolar & hydrophobic? nonpolar & hydrophobic
Effect of different R groups: Polar amino acids polar or charged & hydrophilic Why are these polar & hydrophillic?
Protein Structure Shape determines function in protein structure Each level in structure represents a fold in protein More folds = more complex protein
Primary structure The Amino Acid chain Sequence of amino acids is unique for each polypeptide –Slight changes in AA sequence can result in major differences What determines the AA sequence?
Secondary structure Local folding patterns –α helix –β pleated sheet Result of H bonding between backbone N and O.
Secondary structure Hydrogen Bonding
Tertiary structure Overall 3D shape of the polypeptide –Resulting from the interactions of R groups –Examples: Hydrophobic disulfide bridges (cysteine AA) hydrogen bonds ionic bonds
Quaternary structure Overall PROTEIN structure –More than one polypeptide chain bonded together to form a functional protein
Proteins denature when a protein unravels and loses its native conformation (shape) –Loss of shape = loss of function –Reversible or Irreversible Denaturation Renaturation Denatured protein Normal protein
Protein structure overview 1.Primary –AA seq…bonds? 2.Secondary –Alpha or beta…Bonds? 3.Tertiary –bonds? 4.Quaternary –Multiple polypeptides interact to form functioning protein
FUNCTION Store Genetic Information Transmit Genetic Information “recipe” for Proteins Two Types: –DNA (deoxyribonucleic acid) –RNA (ribonucleic acid) Nucleic Acids
DNA vs. RNA Major Differences: –DNA: deoxyribose sugar, ATCG –RNA: ribose sugar, AUCG
Nucleotide Structure Nucleotides include:Nucleotides include: 1.phosphate group 2.pentose sugar (5-carbon) 3.nitrogenous bases: adenine (A) thymine (T) DNA only uracil (U) RNA only cytosine (C) guanine (G) The only group that changes
Nucleotides Purines: double ring –Adenine –Guanine Pyrimidines: single ring –Thymine –Cytosine G-C=3 hydrogen bondsA-T=2 hydrogen bonds Complementary Base Pairing
Phosphodiester Linkage Between Phosphate group of one nucleotide and 3” OH group of another nucleotide.
ATP…a very special nucleotide!! Adenosine Triphosphate Power to drive cellular reactions ATP functions by transferring its phosphate group to another molecule –creating a phosphorylated intermediate. –phosphorylated intermediate is usually less stable (more reactive) than the original molecule, which drives the reaction