define ORGANIC MOLECULE those that contain CARBON (exs: carbs, lipids, proteins, nucleic acids, & adenosine triphosphate define ISOMER same # of atoms of each element, but different arrangements Carbon always makes how many bonds? 4 name the 7 MAJOR FUNCTIONAL GROUPS hydroxyl sulfhydryl carbonyl carboxyl ester phosphate amino HYDROXYL -OH same as in bases found in alcohols and sugars makes organic molecules water-soluble polar and hydrophilic SULFHYDRYL -SH like hydroxyl, but sulfur+hydgrogen important in protein structure polar and hydrophilic ESTER formed from reaction of acid and alcohol found in fats, oils, also nerve chemical acetylcholine COOC CARBOXYL organic acid (H+ easily donated) also written -COOH usually charged (i.e. -COO-) at cellular pH more oxygen present, more water soluble hydrophilic AMINO acts as base binds H+ to form -NH3+ at cellular pH amino + carboxyl in same molecule is an amino acid amine-anything with Nitrogen NHH PHOSPHATE found in energy-storing molecules and in nucleic acids (DNA, RNA) hydrophilic ex: ATP (adenosine triphosphate) PO42- CARBONYL carbon and oxygen in double covalent bond found in KETONES, formed when fats are broken down water-loving groups (hydrophilic) polar CO arrangements that are commonly found in carbon-containing molecules FUNCTIONAL GROUPS what are the 4 main kinds of biological molecules? carbohydrates (sugars) lipids (fats) proteins nucleic acids define and explain CARBOHYDRATES 5 or 6 carbons "watered carbon" always 1 carbon + 1 water (H2O) formula CxH2xOx (ex: C6H12O6) form ring structures by linking carbons 1 and 5 through an O ratio for carbons-hydrongens-oxygen 1:2:1 carbs ALWAYS have same # of carbons as water molecules define and explain LIPIDS (FATS) carbon, hydrogen, and oxygen (more carbon than oxygen) different proportions than carbs- less O2 (more O2- increased solubility) hydrophobic or non-polar- tend to repel water used to build cell membranes PROTEINS (made up of amino acids) amino acids always contain carbon, hydrogen, oxygen, and nitrogen some amino acids include sulfur NUCLEIC ACIDS sugar "backbone" plus nitrogenous base nitrogenous base with one or two rings one-ring pyrimidines (uracil, thymine, cytosine) two-ring purines (adenine, guanine) deoxyribose backbone: DNA ribose backbone: RNA *your body makes DNA & RNA define MONOMER and give them for each of the 4 main kinds of biological molecules single units carbohydrate- monosaccharide (glucose) protein- amino acid (there are 20) nucleic acid- nucleotide lipid- fatty acid define POLYMER and give them for each of the 4 main kinds of biological molecules result when monomers are bound together in a string or branched structure carbohydrate- polysaccharides protein- polypeptides (after 30, proteins) nucleic acid- DNA & RNA lipid- triglycerides define DEHYDRATION SYNTHESIS "building" (taking water out and making something) combo of 2 monosaccharides with formation of water molecule ALL 4 main kinds of biological molecules are dependent on fromation of bonds by dehydration synthesis (CARBOHYDRATES) define PENTOSE 5 Carbons ribose deoxyribose (CARBOHYDRATES) define HEXOSE 6 Carbons glucose fructose galactose what are the formulas for the disaccharides? glucose+glucose=maltose glucose+galactose=lactose glucose+fructose=sucrose what are your MONOSACCHARIDES? glucose fructose galactose deoxyribose ribose DISACCHARIDES are...? combo of 2 monosaccharides by dehydration synthesis- formed when 2 hexoses combine formed when the -OH of one sugar finds the -H of another and combines to form a water molecule (HOH) sucrose (table sugar)- glucose+fructose lactose (milk sugar)- glucose+galactose maltose- glucose+glucose POLYSACCHARIDES are...? multiple monosaccharides combined by dehyration synthesis exs: ABO blood group markers: glycogen, starch, and cellulose explain the role of PENTOSE SUGARS in forming nucleic acids hexoses are a food source, pentoses are NOT, rather they are essential for structure of nucleic acids (RNA & DNA) ribose and deoxyribose differ because deoxyribose has 1 less oxygen(that's what gives it its name) ribose-backbone for RNA deoxyribose-backbone for DNA what are the 3 major HEXOSES and describe them? glucose- (MOST IMPORTANT!) human cells prefer it as an energy source, is the only significant component of "blood sugar" fructose- found in fruit and honey"fruit sugar" (high fructose corn syrup(HFCS) is glucose converted to fructose by enzymes) galactose- found in dairy products and sugar beets they are all found in significant quanitities in the human diet define HYDROLYSIS "water breaking" opposite of dehydration synthesis, a water molecule is added to sucrose as it is broken into glucose and fructose (what happens inside our cells as table sugar is metabolized in the diet) hydrolysis of scrose is catalyzed by an enzyme invertase (aka sucrase) name the carbohydrate polymers found in plants and describe each polysaccharides(polymers of carbs) long strings of monomers, may be branched or unbranched cellulose- cell walls, NOT digestible (fiber) starch- storage form of glucose(major source of carbs in diet) CAN be digested name the carb ploymer found in humans and describe polysaccharide in humans- GLYCOGEN major storage form of glucose in humans mostly in the liver and MUSCLE (mostly) easily broken down (hydrolysis) to glucose(used to power cells(carb loading)) give one example of a polysaccharide found as a surface marker (for blood ABO) GLYCOLIPID- combo of lipids(phospholipids) and sugar(carbs) groups these sugars mark specific cell types process: polysaccharide is attached to a lipid molecule (one monosaccharide involved is galactose) compare and contrast roles of mono, di, and polysaccharides in human biology (poly) CARBS- most important constituent of human diet- can be used for energy under AEROBIC and ANAEROBIC conditions (poly) starch from plants-important carb source cellulose- "fiber" in diet mono and disaccharides are used as sweeteners show dehydration synthesis and hydrolysis reaction --> dehydration synthesis (building) <-- hydrolysis (breaking) synthesis of triglycerides (polymers for lipids) fatty acids added to glycerol backbone by dehydration synthesis triglycerides are held together because of Ester linkage what are the 6 types/forms of lipids in the body? fatty acids triglycerides phospholipids steroids eicosanoids other lipids (fat soluble vitamins & lipoproteins) explain POLAR vs NON-POLAR polar- charged (+ or - ions) hydrophilic (likes water) non-polar- uncharged (no ions) hydrophobic (hates water) define and describe FATTY ACIDS building blocks of lipids monomers of lipids each ends in a carboxyl(-COOH) group, which is where the "ACID" part comes in there are saturated and unsaturated (poly and mono) fatty acids define SATURATED fatty acids "filled" with hydrogen all the carbons are filled, or saturated, with hydrogen atoms in the zigzag pattern of carbon backbone- its straight solid @ room temp (butter) define UNSATURATED fatty acids "missing" hydrogens when double bonds form between carbon atoms, fewer hydrogens can bond to carbons the double bond puts a "kink" in the regular zigzag patter of carbon backbone monounsaturated= 1 double bond=1 kink polyunsaturated= many double bonds= many kinks (liquid @ room temp-olive oil) define and describe TRIGLYCERIDES 3 fatty acid chains added to a molecule of glycerol to form triglycerides dont need to be same size or saturation, can be any combo GLYCEROL backbone define and describe PHOSPHOLIPIDS formed when 2 fatty acid tails (carbon & hydrogen ONLY) are joined by a glycerol molecule to a phosphate-containing "head group" cell membranes are made up of phospholipids head- polar, hydrophilic- choline neck- polar, hydrophilic- phosphate glycerol- backbone tails- non-polar, hydrophobic- fatty acid (carbon & hydrogen ONLY) molecules define and explain AMPHIPATHIC associated with phospholipids has polar "head" & non-polar "tails" forms lipid bilayers (oreo cookie) found in cell membranes the tails associate (face) with eachother and the heads associate with water define and explain STEROIDS CHOLESTEROL is the basis for this class of molecules (we CAN'T live without it) exs: vitamin D, estradiol(type of estrogen), testosterone, and cortisol define and explain EICOSANOIDS PROSTAGLANDINS & LEUKOTRIENES- "local hormones"- affects sight of damage right there prostaglandins & leukotrienes derive from ARACHIDONIC ACID they are key chemicals in immune defense and inflammation leukotrienes contribute to inflammation associated with asthma prostaglandins contribute to pain/inflammation associated with immune response define and explain FAT-SOLUBLE VITAMINS ADEK vitamin A is synthesized from carotenes- important in vision (signs-poor teeth & gums, night blindness) vitamin D is important in bone formation, cholesterol derivative (sign-rickets (low blood calcium, soft bones, distorted skeleton)) vitamin E is a protective molecule (skin protection) vitamin K is important in blood clotting (sign-slow blood clotting) define and explain LIPOPROTEIN lipid carriers in blood differ in density, have different effects on health lipids are less dense than water (oil floats) VLDL- high lipid content(low protein) Very Low Density Lipoprotein- most damaging form of lipoprotein (BRINGS fats to heart) LDL- intermediate lipid content- Low-Density Lipoprotein HDL- highest protein cotent, lowest lipid content, its believed to exert protective effect, its increased by exercise- High Density Lipoprotein (best one, carries fats AWAY from heart) name the 2 FUNCTIONAL GROUPS on AMINO ACIDS and explain amino acids a little bit 2 carbons and a nitrogen form backbone (middle) amino group- nitrogen is bonded to 2 hydrogens (on side) carboxyl group- carbon, 2 oxygen, hydrogen (other side) (side chain) R & H AMINO GROUP-NH2 when uncharged, NH3 + when charged (ionized) CARBOXYL GROUP- -COOH when uncharged, -COO- when charged (ionized) (R GROUPS- placeholders) all of that together, with dehydration synthesis form peptide bonds (remember the drawing of amino and carboxyl groups and then removing H2O (dehydration synthesis) to form a peptide bond) the result from that is called a dipeptide and more than 2 amino acids is called a polypeptide enzymes, called peptidases or proteases break peptide bonds by hydrolysis 20 AMINO ACIDS- what you NEED to know differ in their R groups & have different chemical properties: polar(hydrophilic) vs non-polar(hydrophobic) acidic vs basic define DISULFIDE BONDS formed from Cysteine, with its -R group containing a sulfhydryl help hold proteins together ONLY AMINO ACID WITH A SULFYHYDROL GROUP simplest amino acid GLYCINE makes bend in amino acid chain (folds back into itself) PROLINE purple box CLOWNS- oddballs (unique) green box GAYS- polar, charged acids (left) & bases (right) blue box BOYS- polar, uncharged- don't share equally in the thyroid, Iodine is added to what? to make thyroid hormones TYROSINE pinkish box GIRLS- non-polar, share equally describe protein PRIMARY STRUCTURE and what are the 2 primary sequences? start of a protein structure (the order in which amino acids are strung together) sequence of amino acids forming its polypeptide chains 2 primary sequences: 1-ELVIS(glutamic acid-leucine-valine-isoleucine-serine) 2-ferret beta-actin which amino acid is always first in every protein? Methionine describe protein SECONDARY STRUCTURE and give examples form a helices(coil)-ex hair(keratin) form pleated sheats(fold)-ex proteins in nature, like spider silk- H bonds and dotted lines amino acids that DON'T have secondary structure are THREADS describe protein TERTIARY STRUCTURE and examples how helices or sheets are arranged in 3D types of atomic ineractions leading to tertiary structure: 1-ionic bonds 2-hydrophobic interactions 3-Van der Waals interactions 4-disulfide bridges 5-hydrogen bonds what are the four levels of STRUCTURE? primary secondary tertiary quaternary describe protein QUATERNARY and examples 2 or more identical subunits *if a change occurs in primary, it will lead to changes in ALL of them define DENATURATION when we disrupt the interactions between bonds, and unfold a protein, leaving the primary structure intact *it destroys secondary, tertiary, & quaternary structures what are the 6 types of proteins & their functions? STRUCTURAL-form structural framework of various parts of the body (collagen, keratin) REGULATORY-funtion as hormones that regulate various physiological processes: control growth and development; as neurotransmitters, mediate response of the nervous system (insulin) CONTRACTILE-allow shortening of muscle cells, which produces movement (myosin, actin) IMMUNOLOGICAL-aid responses that protect body against foreign substances and invading pathogens (antibodies, interleukins) TRANSPORT-carry vital substances throughout the body (hemoglobin) CATALYTIC-act as enzymes that regulate biochemical reactions (salivary amylase, sucrase, & ATPase) define an ENZYME proteins that speed up (catalyze) chemical reactions proteins that are needed in ALL cells they lower the amount of energy needed to start the reaction, but not the overall energy profile define ACTIVATION ENERGY energy needed to make alignment happen explain ENZYMES ARE CATALYSTS CATALYSTS make reactions go faster, but are NOT CONSUMED the substance undergoing the reaction= SUBSTRATE (TARGET) enzymes are specific (like puzzle pieces) what are the 3 things about enzymes? 1-speed up 2-specific 3-don't consume (reusable) what are the bases and sugars in DNA & RNA? DNA- bases: Adenine, Cytosine, Guanine, & Thymine sugar-deoxyribose RNA-bases: Adenine, Cytosine, Guanine, & Uracil sugar-ribose what are the 3 units/parts of NUCLEOTIDES a base a sugar a phosphate group what are the PYRIMIDINES? URACIL, CYTOSINE, & THYMINE (CUT THE U) what are the PURINES? GUANINE & ADENINE name the key structural features of DNA consists of 2 twisted strands (double helix) used to transmit genetic information backbone- sugar(deoxyribose) + phosphate always in those pairs: (3 hydrogen bonds) cytosine>(chewing gum) C-G base pair guanine (2 hydrogen bonds) adenine>(apple tree) A-T base pair thymine hydrogen bonds between bases hold strands together name the key structural features of RNA unstable used for temporary storage & manipulation of genetic info (scratchpad) does NOT form double helices- single strand backbone-sugar(ribose) + phosphate cytosine guanine adenine uracil explain biological role of ATP (adenosine triphosphate) and how it's used to produce cellular energy energy currency in a subcellular compartment (mitochondrion), oxygen & glucose are converted cellular energy, which is then stored as high-energy phosphate bonds in a molecule(ATP) what are the 5 forms of CELLULAR ENERGY? ELECTRICAL- nerve impulses HEAT- cellular chemical reactions MECHANICAL- muscle contractions POTENTIAL(chemical)- energy-rich covalent bonds RADIANT- photosynthesis in plants define and explain WATER SOLUBLE VITAMINS VITAMIN C- collagen synthesis in connective tissues (signs scurvy (bleeding gums, loose teeth, swollen joints; slow wound healing; weight loss)) VITAMIN B explain vitamins as cofactors in enzymatic reactions need vitamins to assist or work with enzymes to facilitate better work give element, function, & human deficiency signs of MINERALS FLUORINE- structure of teeth/bones, effect on cells which build or break down bone; inhibits microorganisms which degrade teeth(signs-increased incidence of dental caries; osteoporosis) CHROMIUM- efficient use of insulin(signs-relative insulin resistance; impaired glucose tolerance; elevated serum lipids) IRON- oxygen & electron transport; heme group of hemoglobin(signs-anemia) IODINE- constituent of thyroid hormones(signs-goiter; depression of thyroid function; (if congenital) cretinism)