BMS 110 Unit 1 Ch. 2 Molecules of Life

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FlashCards sobre BMS 110 Unit 1 Ch. 2 Molecules of Life , criado por Makenna Ornes em 17-09-2021.
Makenna Ornes
FlashCards por Makenna Ornes, atualizado more than 1 year ago
Makenna Ornes
Criado por Makenna Ornes aproximadamente 3 anos atrás
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Questão Responda
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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