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Erstellt von Makenna Ornes
vor fast 3 Jahre
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Frage | Antworten |
biological molecules | compounds built in atoms of element carbon; organic compounds |
four main biological molecules | carbohydrates, lipids, proteins, nucleic acids |
organic compounds | contain carbon & at least 1 hydrogen atom |
inorganic compounds | doesn't have both carbon & hydrogen ex: water (H2O) |
what behavior does carbon have? | versatile bonding behavior |
what is versatile bonding behavior? | each carbon atom can share pairs of electrons with as many as 4 other atoms; covalent bonds are fairly stable because carbon atoms share electrons equally |
angles of covalent bonds produce... | shape of organic compounds |
hydrocarbon | carbon backbone with only hydrogen atoms attached to it |
functional groups | an atom/cluster of atoms that are covalently bonded to carbon -kind, arrangement, # determines specific properties such as polarity or acidity |
two types of reactions | condensation (anabolic) hydrolysis (catabolic) |
condensation reaction | 2 covalently bonded into larger one -building process -water as byproduct (aka anabolic) |
hydrolysis reaction | molecule splits into 2 small ones, releasing water -breaking down reaction -water as substrate (aka catabolic) |
condensation more in detail | -enzymes remove a hydroxyl group from 1 molecule & an H atom from another & speed formation of covalent bond between the 2 molecules -discared hydrogen & oxygen atoms may from water (called dehydration synthesis) |
polymer | large molecule build of 3 or more subunits (monomers) |
hydrolysis more in detail | -enzymes act on particular functional groups & split molecules into 2 or more parts -enzymes attach an OH- group & a H atom from water molecule to exposed sites |
3rd type of metabolic reaction | relocating/rearranging functional groups |
relocating functional groups reaction | -one molecule gives up functional group that immediately is attached to another molecule -transfer changes structure/function of both molecules involved -electrons may also move from molecule to molecule |
monomers of the biological molecules | carbohydrates - monosaccaharides lipids - glycerol + free fatty acids proteins - amino acids nucleic acids - nucleotides |
carbohydrates main ideas | -consist of carbon, hydrogen, & oxygen in 1:2:1 ratio -most abundant & most readily available -used for energy; most preferred |
3 major classes of carbohydrates | monosaccharides, oligosaccharides, & polysaccharides |
monosaccharides | -simplest carbohydrate, simplest sugar -has at least 2 OH- groups joined to carbon backbone plus an aldehyde or ketone group -backbone of 5 or 6 carbons -taste sweet & dissolve easily in water |
main examples of monosaccharides | glucose, fructose, galactose |
glucose | -monosaccharide -main source of energy for body cells; has 6C 12H -building block for larger carbohydrates -parent molecule (precusor) for many compounds like Vitamin C, dervied form sugar monomers |
oligosaccharides | -short chain of 2 or more sugar monomers that are joined by dehydration synthesis -disaccharides consist of 2 sugar units -proteins/other large molecules often have oligosaccharides attached as side chains |
main examples of oligosaccharides | raffinose & stachyose |
main examples of disaccharides | sucrose, lactose, & maltose |
lactose | -disaccharide -a glucose & a galactose unit -milk sugar |
sucrose | -disaccharide -most plentiful sugar in nature; simple sugar -consists of 1 glucose & 1 fructose unit -in fruits, table salt, other plant foods |
maltose | -disaccharide -found in alcohol, bread |
polysaccharides | -straight/branched chains of sugar monomers; "complex" carbohydrates -often 1000s joined by dehydration synthesis -store energy; energy released to cells when sugar is broken down -make up most carbohydrates we eat |
main examples of polysaccharides | starch, glycogen, cellulose, & chitin |
cellulose | -plants store large amount of glucose in form of cellulose -humans don't have digestive enzymes to break down cellulose in whole grains, fruits, vegetables, etc. -undigested fiber adds bulk & helps more wastes through lower part of digestive tract |
many plant derived foods are rich in... | starch |
glycogen | -polysaccharide one way animals store sugar (in muscles & liver) -person's blood sugar decreases, liver cells break down glycogen & release glucose to blood -quick source energy |
lipids main ideas | -nonpolar hydrocarbon -hydrophobic; dissolves easily in nonpolar substances -fats = largest reserve store of energy |
uses of lipids | -store energy -signal molecules -structural materials -phospholipids build cell membrane |
fats | -largest reserve store of energy -lipid with glycerol head & 1, 2, or 3 fatty acid tails -fatty acid has backbone up to 36 carbons & a carboxyl group (-COOH) at one end |
saturated fats & examples | -solid at room temp -fatty acid backbones only have single covalent bonds -ex: butter, lard, chicken fat |
unsaturated fats & examples | -liquid at room temp -fatty acid backbones have 1 or more double covalent bonds -bonds have rigid kinks to prevent from packing tightly -some are unhealthy (ex: trans fat) -ex: vegetable oils like canola oil, peanut oil, corn oil, olive oil |
triglycerides | -neutral fat; most common & richest source of energy -lipid containing 3 fatty acid tails attached to glycerol backbone -yield twice as much energy than complex carbohydrates (have more removable electrons than do carbohydrates (energy released when electrons are removed)) -specialized storage: adipocytes -stored as fat droplets in fat-storing tissues |
examples of triglycerides | butter, lard, oils, other dietary fats consist mostly of these |
phospholipids | -glycerol backbone, 2 fatty acids tails, hydrophilic "head" with a phosphate group & another polar group -main materials of cell membranes which have 2 layers of lipids -fatty acid tails = hydrophobic |
sterols | -lipid with no fatty acid tails & a rigid backbone of 4 fused-together carbon rings -components of membranes -differ in #, position, & type of their functional group -associate sterol cholesterol with heart disease -precursors of steroid hormones |
derivatives of cholesterol | Vitamin D (bone/tooth development), bile salts (fat digestion in small intestine), & steroid hormones (estrogen & testosterone) |
proteins main ideas | -most diverse -organic compound built of 1 or more amino acid chains -20 kinds of amino acids -do work inside/outside cells -catalysts, enzymes, tension/torsion, signaling -TOOLS of the body |
enzymes | proteins that speed up reactions |
structural proteins | building blocks of cells & tissues in bones, muscles, etc. |
types of proteins & functions | -transport proteins move substances -hormones adjust cell activities -others important in body defenses |
amino acid | small organic compound (central carbon atom) that consists of... 1) an amino group (-NH2) 2) a carboxyl group (-COOH, an acid) 3) hydrogen atom 4) R group/side chain (1 or more atoms) -1, 2, 3 stay same on all amino acids -linked by peptide bonds |
R groups | -radical side chain -help determine an amino acid's chemical properties -are unique in every amino acid |
peptide bonds | -COVALENT bond that joins amino group of 1 amino acid to carboxyl group of 2nd amino acid |
dipeptide bond | when peptide bonds join 2 amino acids together |
polypeptide chain | -when peptide bonds join 3 or more amino acids together -each has unique sequence of amino acids -DNA determines order in which amino acids are added to chain |
primary structure | particular sequence of amino acids that make up a protein |
when amino acids are done assembling into protein, protein... | folds into its final shape |
a protein's final shape determines... | its function |
protein's primary structure streps | 1) formation of functioning protein 2) structure emerges as chain twists 3) its structure changes, hydrogen bonds form between amino acids in different parts of chain |
what determines a protein's final shape? | sequence of amino acids; folding/interacting of amino acids |
aspects of secondary structure | -hydrogen bonding -alpha helix -beta pleated sheet |
tertiary structure & example | -what makes protein a molecule that can perform a function -continued hydrogen bonding -disulfide bridges (covalent) -tucking away hydrophoic amino acids -ex: hollow "barrel" provides a channel through which substances can move in/out of cells |
quaternary structure & example | -proteins built of 2 or more polypeptide chains -hydrogen bonds hold chains together -ex: hormone insulin & hemoglobin (protein in RBCs - 4 molecules of globin & iron-containing functional group) |
collagen | most common protein in body -elongated, strong, fibrous |
2 types of final shape of proteins & what are they | -fibrous = stringy, touch, usually insoluble in water -globular = round, usually water soluble |
lipoproteins | -form when certain proteins in blood combine with cholesterol, triglycerides, & phospholipids that were consumed in food -lipids are attached |
glycoproteins | oligosaccharides are attached -most proteins found on surface are glycoproteins & they are many of the proteins in blood & cells that secrete (protein hormones) |
denatured & example | when protein/other large molecule loses its normal 3D shape -ex: temp or pH exceeds protein's tolerance, hydrogen bonds break, polypeptide chains unwind/change shape, protein no longer functions |
nucleotide | composed of... 1) 1 sugar (ribose or deoxyribose) 2) at least 1 phosphate group 3) 1 nitrogen-containing base (adenine, guanine, cytosine, thymine) |
ribose | 5-carbon ring structure, 2 oxygen atoms attached to ring |
deoxyribose | 5-carbon ring structure, 1 oxygen atom attached to ring |
ATP | adenosine triphosphate; row of 3 phosphate groups attached to sugar -links chemical reactions that release energy with other reactions that require energy -can transfer a phosphate group to other molecules in cell providing them with energy |
coenzymes | "enzyme helpers"; move hydrogen atoms & electrons from one energy reaction sit to another |
cAMP | cyclic adenosine monophosphate; acts as chemical messenger in & between cells |
nucleic acids | long single-stranded or double-stranded chain of 4 different nucleotides joined at phosphate groups |
DNA | -nucleotide; deoxyribonucleic acid -double-stranded -thymine -bases: A, T, C, G |
RNA | -nucleotide; ribonucleic acid -single-stranded -uracil -regulates cellular metabolism, produces proteins, governs developmental timing -bases: A, U, C, G |
DNA contains genetic info to... | 1) build proteins 2) regulate physiological processes 3) maintain homeostasis |
most energy is available in... | spurts (it is not a continuous system) |
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