Biology Chapter 2

Substance that produces or yeilds hydrogen (H+) when put into another solution

Dairy products, oven cleaner, bleach, oxygen, grease

Substance that accepts Hydrogen (H+)

Usually Non Polar

• Structure is balanced and symetrical.
• -Usually in covalent bonding?
• -Generally Hydrophobic
• -Don't mix with polar substances because polars have charges and non polars dont?

Type of Element but with different number of neutrons. Same number of protons and electrons. Different structure

-same molecular formula but different structure

• Non Polar
• -Can change non polar molecules by adding a functional group.
• -It will change the charge, making it charged and thus making it polar (changes its polarity) And so its bonding capabilities are changed

• -OH hydroxide group (found in sugars and alcohols)
• -COOH carboxyl group (found in fatty acids and amino acids)
• -NH v2 Amino Group (found in Amino Acids)
• -Phosphate Group (energy) (found in ATP, DNA, RNA)

• -Sugars
• (4 kinds)
• -Monosaccharides-single sugars (glucose, fructose)
• -Disaccharides - 2 sugars (lactose, sucrose)
• -Polysaccharide- 3 or more sugars linked together

single repeating unit/ 3 or more monomers

a monomer is a pearl and a polymer is a string of pearls

• -Simple Sugars that cannot be broken down by hydrolysis into smaller sugars.
• -Glucose and Fructose C6H12O6
• -main fuel molecules for cellular work (particularly glucose)
• -provide cells with carbon skeletons that can be used for raw material for manufacturing other kinds of organic compounds

• -Double sugar constructed from 2 monoscaccharides through a dehydration reaciton.
• -Lactose, maltose (alcohol, malted milk shakes), sucrose (plant sap)
• -Lactose: glucose and galactose
• -Maltose: two glucose
• -Sucrose: glucose and fructose

• -Complex Carbohydrates
• -Long chains of sugar units- polymers of monosaccharides
• -Starch: many glucose monomers strung together
• -for plants its stored for when it can be broken down as needed to provide energy and raw material for building other molecules.
• -Starch: potatoes, grains like wheat, corn, and rice
• -Glycogen: excess sugar stored by animals. Structure like Starch (both polymers of glucose monomoers) Glycogen is more extensively branched. Used for Energy and "carbo loading"
• -Cellulose: most abundant organic compound on Earth. Enclose plant cells and is in wood. STRUCTURE Resembles starch and glycogen structure too. Dietary Fiber because most animals can't break it down. Hydrophilic

• Starch: Found in plants, seeds, and roots. STORAGE
• Glycogen: STORAGE, found in animals in their muscles and liver
• Cellulose: STRUCTURE, Plants
• Chitin: STRUCTURE, exoskeleton of insects

• -Unlike carb's, these are Hydrophobic.
• -fats
• -steroids
• -Waxes: found in plants
• -phosopholipids: found in membrane, have phosphate head: carboxy group at end so that it can bond
• -triglycerides: storage form of fat (90% of fat in our bodies)

• -typical fat cosists of a glycerol molecule joined with 3 fatty acid molecules through dehydration reactions. This makes a Triglyceride.
• -has more energy than a carbohydrate
• -major portion of a FA is a long hydrocarbon that stores a lot of energy
• -stored in adipose cells, tissue or "body fat:
• -saturated and unsaturated fatty acids

• a hydrocarbon chain with a carboxyl group at end to change it from non polar to polar so it can bond.
• -bonding occurs when a gylcerol and a fatty acid link.
• -fatty acids are Hydrophobic

• -fatty acid that has fewer than the max number of hydrogens at the location of the double bond (where it bends)
• -Unsaturated Fat: one with one or more unsaturated fatty acid tails
• -Polyunsaturated fat has several double bonds within its fatty acids
• -The more Unsaturated The more Liquid at room temp it is
• -animal fats, lard, butter, meat, cheese
• -Liquid because the FA tails aren't straight and therefore can't pack together to form a solid at room temperature

• Fatty Acid
• -Chain that does not bend
• -contain the max number of hydrogen atoms.
• Saturated Fat
• -one with all 3 of its fatty acid tails saturated
• -plants and fish fats , oils, trans fat, margarine
• -Solid because the FA tails are straight so they can fit together closer and pack in more, making a solid

• -Used by manufacturers to convert unsaturated fats to saturated fats by adding hydrogen
• -creates Trans Fat

-chemical reaction where it bubbles Hydrogen (when heated) through the oil. It breaks the bonds, adds hydrogen in it makes the fatty acid tails straighten out where they have the bends

• -Completely Saturated Fat (solid at room temp)
• -They can come together to get harder like plywood, making it solid (sat fat)
• -Form that your body stores fat before it gets broken down

Structure is an E figure : Glycerol + 3 Fatty Acid Tails

• -glycerol + 2 fatty acids + phophate head
• -fatty acids move away from water and polar head face the extra cellular water and cellular fluid
• -polar heads attracte to outter phosphate heads
• -doesn't allow most polar molecules through. A little water goes throug the barrier but not a lot

• -classified as lipid because they're hydrophobic.
• -have carbon skeletons that are bent to form 4 fused rings
• -Function is determined by the Functional Groups attached to these rings
• -cholesterol: essential molecule that is a key component of the membranes that surround our cells. And "base steroid" from which our bodies produce other steroids like estrogen and testosterone.

• -most elaborate of life's molecules
• -protein= polymer constructed from amino acid monomers.
• -3 dimensional shapes corresponding to a specific function
• -perform most of the tasks required for life
• -most important role as enzymes: chemicals that change the rate of a chem reaction without being changed int he process.
• -Lactase
• -protein= polymer consisting of one ore more polypeptides (long chain of amino acids that are bonded together through peptide bonds)
• -Ribosomes: are proteins

• -20 Amino Acids
• -For structure support, and skeletal, also used for immunity, cellular structure
• -transport proteins from one side to another (like oxygen transported in blood by protein)
• -enzymes: help break/build things at a faster rate
• -Joined together by Peptide Bonds

• -consist of central carbon atom bonded to 4 covalent bonds
• -3 of those attachements are common to all 20 amino acids: a carboxyl group, an amino acid group, and a hydrogen atom. The 4th bond is what determines the type and special chemical properties (side group)

Structure Proteins: Provide Support, give hair and horns their toughness

Storage Proteins: Provide amino acids for growth, seeds and eggs are rich in storage proteins

Contractile Proteins: Help movement, contractile protiens enable muscles to contract

Transport Proteins: help transport substances, protein hemoglobin within red blood cells transports oxy

Enzymes: help chemical reactions, some cleaning products use enzymes to help break down molecules

• Primary: Amino Acid Sequence, each protein's unique linear sequence of amino acids
• Secondary: (where you get hair and nails) B- pleated sheet www (zig zag form) -alpha helix (winding staircase form) -random coil

• Tertiary Stucture: 3-d Structure (the three secondary forms mixed together)
• - having hydrogen bonding and different interactions to get these, turns into the middle because it's afraid of the water, has to do with covalent, ionic, and hydrogen bonding, as well as wtih hydophobic and hydrophilic properties.

Quaternanry Structure: 2 tertiary's or more come together

• -an unfavorable change in temp, pH, or some other quality of the environment can cause a protein to unravel and lose its normal shape. called denaturation of a protein.
• -like when you cook an egg and the egg white turns from clear to white.
• -the denatured proteins become insoluble in water and form a white solid.
• -why fevers over 104 deg are dangerous because some of our protiens denaturate above that

• Macromolecules that provide the directions for building proteins.
• -in the nuclei of eukaryotic cells
• -2 Types:
• -DNA: deoxyribonucleic acid (resides in the cell as one or more very long fibers called chromosomes).
• -RNA: ribonucleic acid (help translate the chemical code that must be translated from "nucleic acid language" to "protein language"
• -Gene: a specific stretch of DNA that programs the amino acid sequence of a polypeptide. within the cell, it provides the directions to build a molecule of RNA which can then be translated into a protein.
• -polymers made from monomers called nucleotides

• -monomers that make up polymers (nucleic acids)
• -each contains 3 parts. at the center of each is a 5-carbon sugar, deoxyribose in DNA and ribose in RNA. Attatched to the sugar is a - charged phosphate group containing a phosphorus atom bonded to oxy atoms (PO4-) Also attached to the sugar is nitrogenous (nitrogen containing) base made of one or 2 rings. called a base because it accepts hydrogen atoms in aqueous solutions.
• -the sugar and phosphate are the same in all nucleotides; only the base varies
• -Each DNA nucleotide has one of 4 nitrogenous bases: adenine (A), guanine (G), cytosine (C), or thymine (T)

• -RNA: sugar is ribose instead of deoxyribose.
• -RNA has base uracil (U) and DNA has thymine

• -a RNA polynucleotide chain is identical to a DA polynucleotide chain other than these differences
• -Rna is usually found in single-stranded form and DNA is usually as a double helix

• -animals/ plants
• -complex
• -compartmentalize/ organelles
• -nucleus with DNA
• -need oxygen

• -bacteria
• -simple
• -no nucleus
• -anaerobic (need no oxy)/ aerobic (need oxy)

Nucleus: DNA and RNA

Ribosome: made of protein and rRNA-2 subunits

Dna makes RNA -- Goes through nuclear pores -- goes to ribosome--binds with half of a mRA -- sub units come together --- builds amino acid ---and thus builds a protein---then ER

Endoplasmic Reticulum: responsible for protein folding, quality control, and sugar tags (gycosylation, adding sugar to protein and acts as label)

• then gets sent to Golg: Apparatus: distribution center when passes quality control. then it gets sent to where it needs to go
• if it fails quality control in ER, then it gets sent to Lysosome, where it gets broken down with enzymes to amino acids, responsible also for cells that are no longer working. then they get sent to cytooplasm to ge re-used.