CHAPTER 5- The Structure and Function of Large Biological Molecules

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1 CHAPTER 5- The Structure and Function of Large Biological Molecules CARBOHYDRATES = sugars and their polymers FUNCTIONS: *Energetic fuel source/storage *Structural building blocks MONOSACCHARIDES: C, H, O in 1:2:1 ratio (CH 2 O) n 3-7 carbons Pentoses (5C) & hexoses (6C) most common; but glycerol (3C) also important OH attached to each carbon except one Major nutrient for cells names often end with -ose. Aldehydes (=O at end) form OR ketones (=O in middle) *Glucose & fructose = structural isomers *Glucose & galactose = stereoisomers *All = (C 6 H 12 O 6 ) DISACCHARIDES: *2 monosaccharides joined together by a condensation (dehydration synthesis) reaction *bond is a GLYCOSIDIC linkage (covalent) Sucrose = glucose + fructose Maltose = glucose + glucose Lactose = glucose + galactose POLYSACCHARIDES long polymers of monosaccharides (few 100-few 1000) formed by condensation (dehydration synthesis) reaction Numbers identify the linked carbons and form of glucose STARCH - energy storage in plants (EX: potatoes) GLYCOGEN energy storage in ANIMALS Stored as cytoplasmic granules in liver and muscle Liver controls blood sugar level Ex) low blood sugar between meals (glycogen glucose) (GLUCAGON) Ex) high blood sugar after eating (glucose glycogen) (INSULIN) Muscle tissue- source of ATP for muscle contraction

2 CELLULOSE major component in plant cell walls (EX: wood, cotton) straight unbranched chains Form MICROFIBRILS that give cellulose its structural rigidity Dietary fiber in human diet Can t be digested by animals without the help of symbiotic microorganisms Don t have enzymes to break linkages CHITIN: Support and protection EX: Cell walls in fungi; exoskeletons in arthropods LIPIDS = diverse group of hydrophobic molecules Many nonpolar C H bonds/long hydrocarbon skeleton Hydrophobic - insoluble in water (dissolve in nonpolar solvents) FATS = TRIACYLGLYCEROL = TRIGLYCERIDE store large amounts of energy NOT polymers but assembled from smaller molecules by dehydration synthesis reactions Adipose tissue is made primarily of triacylglycerols (fat) FAT = 1 glycerol + 3 fatty acids FATTY ACID: Hydrocarbon chain of carbons in length Fatty acids vary in length (number of carbons) and in the number and locations of double bonds Three fatty acids can be the same or different SATURATED - no double bonds in carbon chains Form straight chains Most animal fats are saturated (butter, lard) Solid at room temperature UNSATURATED one/more double bonds in tails have kinks wherever there is a double bond prevents tight packing of molecules so not solid Plant and fish fats = liquid at room temperature = oils (olive oil, cod liver oil) POLYUNSATURATED = many double bonds

3 FUNCTION - (fats, oils) - ENERGY STORAGE Compact energy storage; energy stored in C-H bonds; about 3X the energy of carbohydrates Humans and other mammals store fats as long-term energy reserves in adipose cells Adipose tissue also functions to cushion vital organs, such as the kidneys A layer of fat can also function as insulation (especially in whales, seals, and most other marine mammals) PHOSPHOLIPIDS FAT with one fatty acid replaced by a phosphate group The phosphate group carries a negative charge Additional sugars, amines, or other groups may be attached to the phosphate group to form a variety of phospholipids Heads are often zwitterions: they have both + and -charge. AMPHIPATHIC Both phobic AND philic parts polar head non-polar tails ADDING PHOSPHOLIPIDS TO WATER self-assemble into MICELLES sphere with hydrophobic tails toward interior polar/philic heads toward outside environment. FUNCTION OF PHOSPHOLIPIDS Major component in cell membranes Arranged as a bilayer Hydrophilic heads toward the outside of the bilayer in contact with the aqueous solution Hydrophobic tails point toward the interior of the bilayer away from aqueous solution Forms a barrier between the cell and the external STEROIDS Lipids with a carbon skeleton with four fused rings and a small ACYL (carbon chain) tail Insoluble in water (nonpolar) Different steroids vary in the functional groups attached to the rings CH 3 CH 3 OH

4 CHOLESTEROL Important precursor for all other steroids Hormones: cortisone, cortisol, testosterone, estradiol, estrogen Cholesterol also found in animal cell membranes Synthesized in the liver Obtained in the diet (meat, cheese, eggs) Essential in animals, but high levels of cholesterol in the blood may contribute to cardiovascular disease (atherosclerosis) Negative effect of saturated fats and trans-fats due to their impact on cholesterol levels - LDL's (low density lipoproteins) 'bad' cholesterol (deposits in coronary blood vessels) - HDL's (high density lipoproteins) 'good' cholesterol WAXES - protective, waterproof coatings fur, feathers, and skin leaves/fruits of plants insect exoskeletons PROTEINS = Cellular toolbox Proteios = Greek first place Make up 50% or more of dray mass of most cells Humans have tens of thousands of different proteins Typical protein = amino acids; biggest known = 34,000 Know the amino acid sequences of > 875,000 proteins/3d shapes of about 7,000 Scientists use X-ray cystallography to determine protein conformation A protein s function = EMERGENT PROPERTY determined by its conformation EXAMPLES OF VARIETY OF PROTEINS/FUNCTIONS: Structural: hair, fingernails, bird feathers (keratin); spider silk; cellular cytoskeleton (tubulin & actin); connective tissue (collagen) Storage: egg white (ovalbumin); milk protein (Casein); plant seeds Transport: Transport iron in blood (hemoglobin); Hormonal: Regulate blood sugar (insulin) Membrane proteins (receptors, membrane transport, antigens) Movement: Muscle contraction (actin and myosin); Flagella (tubulin & dynein); Motor proteins move vesicles/chromosomes Defense: Antibodies fight germs Enzymatic: Enzymes act as catalysts in chemical reactions Toxins (botulism, diphtheria) AMINO ACIDS *Central (α carbon) with carboxyl, amino, H, and R groups attached *20 common amino acids used by living things

5 POLYPEPTIDE = polymer of amino acid subunits connected in a specific sequence An enzyme joins the carboxyl of one amino acid and the amino group of another via dehydration synthesis/condensation reaction to form a PEPTIDE BOND Peptide bonds are rigid, planar structures The -NH bond and the -C=O bond, point away from each other so these groups can hydrogen bond to other parts of chain LEVELS OF PROTEIN ORGANIZATION/3-STRUCTURE Primary Structure: unique sequence of amino acids; determined by DNA code; unique for each protein Secondary Structure: Determined by amino acid sequence; HYDROGEN BONDS (between the oxygen of C=O and the hydrogen of N-H of peptide bonds) stabilize structure & form pattern α helix- polypeptide chain winds clockwise like a spiral staircase EX: KERATIN, the main protein component of hair, nails, horns β pleated sheet- chains joined together like the logs in a raft EX: SILK Tertiary Structure: Hydrogen bonding, ionic interactions, hydrophobic interactions, and disulfide bridges between R groups stabilize 3 D shape DISULFIDE BRIDGES =COVALENT BOND between amino acids w/-sh groups (CYSTEINE but not methionine) forms an -S-S- bridge SIDE NOTE: Perms work by breaking and reforming disulfide bridges in a new hair shape HYDROPHOBIC INTERACTIONS Polar R groups-interact with water and lie on the surface of the protein Nonpolar R groups - hide in the core of the folded protein polar outside; nonpolar in.side IONIC INTERACTIONS between +/ charged amino acids - -=glutamate, aspartate + = lysine, arginine, histidine HYDROGEN BONDING Some R groups able to form Hydrogen bonds Helps stabilize 3D structure hydrophyllic hydrophobic ionic + - S S S disulfide Quaternary Structure: protein made up of more than one amino acid chain hydrogen EX: COLLAGEN EX:HEMOGLOBIN 3 polypeptides chains twisted in super coil 4 polypeptides

6 WHAT DO YOU CALL IT? two or more amino acids bonded together = PEPTIDE chain of many amino acids = POLYPEPTIDE complete folded 3D structure = PROTEIN Final overall protein shapes - FIBROUS. - long fiber shape EX: actin or collagen - GLOBULAR - overall spherical structure EX: hemoglobin, MUTATIONS CAN CHANGE PROTEIN SHAPE Since shape is determined by amino acid sequence; changing sequence changes 3D shape EX: Sickle cell anemia mutation changes one amino acid in the sequence (glu ala) Abnormal hemoglobin molecules crystallize; cause blood cells to become sickle shaped FACTORS AFFECTING CONFORMATION Folding occurs as protein is synthesized, but physical/chemical environment plays a role DENATURATION: = unraveling/ loss of native confirmation makes proteins biologically inactive ~ Reason high fevers can be fatal does NOT break peptide bonds so primary structure remains intact may regain its normal structure if conditions change sometimes = irreversible (ie. cooking an egg) CAUSED BY changes in ph (alters electrostatic interactions between charged amino acids) changes in salt concentration (does the same) changes in temperature (higher temperatures reduce the strength of hydrogen bonds) presence of reducing agents (break S-S bonds between cystines) NUCLEOTIDES AND NUCLEIC ACIDS INFORMATION FLOW IN CELLS = Central Dogma of Molecular Biology DNA RNA PROTEINS FUNCTION DNA - genetic code contains info that programs cell activities RNA - carries message from DNA to cell; protein synthesis BASIC STRUCTURE NUCLEOTIDE = nitrogenous base + sugar + phosphate group PURINES = 2 rings; Adenine (A), Guanine (G) PYRIMIDINES = 1 ring; Cytosine (C), Thymine (T), Uracil (U)

7 NUCLEIC ACIDS (DNA & RNA) DEHYDRATION SYNTHESIS forms polymers of nucleotide building blocks PHOSPHATES and SUGARS form backbone PHOSPHATE LINKAGE between carbon 3 of one sugar and carbon 5 of the next

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