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68 Cards in this Set
- Front
- Back
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covalent bond
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sharing of electron pairs
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ionic bond
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attraction of opposite charge
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hydrogen bond
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sharing of H+ atoms due to different electronegativities
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hydrophobic interaction
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nonpolar substances interacting in the presence of a polar substance (aggregation)
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Van der waals interaction
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brief interactions of electrons of nonpolar substances
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chemical bonds
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5: covalent, ionic, hydrogen, hydrophobic, Van der waals
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protein
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monomer: amino acid
bond: peptide polymer: polypeptide chain |
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nucleic acid
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nucleotides
phosphodiester linkage nucleic acid? |
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carbohydrates
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monosaccharides
glycosidic linkages (alpha/beta) polysaccharide |
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lipids (fats/oils)
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3 fatty acid/1 glycerol: triglyceride
ester triglyceride |
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lipids (phospholipids)
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2 fatty acids, 1 phosphate, 1 glycerol
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solid ice
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less tightly packed rigid crystalline structure so less dense
floats so bodies of water to not freeze from bottom up and kill life acts as insulating layer to reduce heat flow to cold air above |
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properties of water
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high heat of vaporization, evaporative cooling, high specific heat capacity, cohesion
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heat of vaporization
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amount of heat required to change water from liquid to gas state
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sweating?
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evaporative cooling: body heat is used to evaporate sweat from skin
caused by high heat of vaporization |
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heat specific heat
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the amount of energy required to raise the temperature of 1 g of water by 1 deg celsius
leads to ability of water to moderate climate, minimize temp variations |
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cohesion
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water molecules resist coming apart from one another - hydrogen bonding
allows for water to move through plants results in surface tension |
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two isomeric forms of amino acids
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D-amino acids
L-amino acids (this one in proteins) |
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nonpolar
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isoleucine, leucine, methionine, valine
Ile(I), Leu(L), Met(M), Val(V) |
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polar
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threonine
Thr(T) |
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basic
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histidine, lysine
His(H), Lys(K) |
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aromatic
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phenlyalenine, tryptophan, tyrosine
Phe(F), Trp(W), Tyr(Y) |
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disulfide bond
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applies to the cysteine amino acid in which terminal -SH reacts with adjacent -SH group of another cysteine amino acid to form a covalent bond called a DISULFIDE BRIDGE
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peptide linkages
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condensation reactions in which amino group of one amino acid reacts with carboxyl group on another amino acid. PEPTIDE LINKAGE/PEPTIDE BOND FORMS
Goes from N terminus to C terminus |
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primary structure
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sequence of amino acids in a polypeptide chain held together by peptide linkages - COVALENT BONDING
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HTR S/S
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jaundice, no increase in Hb, hemoglobinuria
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alpha helix
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R groups extend outward from the peptide backbone of helix; coiling results from hydrogen bonds that form between delta pos hydrogen of N-H of one amino acid with delta pos hydrogen of C=O of another
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beta pleated sheet
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formed from two or more polypeptide chains that are almost completely extended and aligned; stabalized by hydrogen bonds between N-H groups on one chain and C=O groups on the other
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tertiary structure
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polypeptide chain is bent at specific sites and then folded back and forth, resulting in macromolecule with 3-D shape
interactions between R groups determine tertiary structure called subunit |
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types of interactions
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1. covalent disulfide bridges: form between specific cysteine side chains
2. hydrogen bonds: between side chains to stabalize folds 3. hydrophobic side chains: can aggregate together in the interior of a protein away from water, folding polypeptide in the process 4. van der Waals forces: stabalize close interactions btw hydrophobic side chains 5. ionic bonds: can form btw +/- charged side chains forming salt bridges |
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quaternary structure
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results from the ways in which subunits (polypeptide chains) bind together
hydrophobic interactions, van der Waals forces, ionic bonds, hydrogen bonds hemoglobin pockets for iron to bind |
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denaturation
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secondary and tertiary structures affected by (1) high temp, (2) pH changes, (3) high concentrations of polar molecules
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high temp
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cause rapid molecular movement that can break hydrogen bonds and hydrophobic interactions
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pH change
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can change pattern of ionization of carboxyl and amino groups in the R groups of amino acids, thus disrupting the pattern of ionic repulsions and attractions
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high concentrations of polar molecules
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disrupt hydrogen bonding that is crucial to structure
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carbohydrates
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molecules in form H-C-OH used an energy source, carbon skeleton
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monosaccharide
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monomer; simple sugar
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disaccharide
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two monosaccharides covalently linked
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oligosaccharide
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3-20 monosaccharides
ABO blood types |
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polysaccharides
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hundreds/thousands of monosaccharides
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glucose
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monosaccharide used to transport energy in humans, used as energy source in cells STRAIGHT CHAIN AND RING FORM
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beta-D-glucose RING FORM
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OH pointing up
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alpha-D-glucose RING FORM
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OH pointing down
ad alphabetical order |
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deoxyribose, ribose
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oxygen removed from OH on second carbon in deoxyribose (both pentoses)
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sucrose
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disaccharide formed by the alpha 1,2 glycosidic linkage btw alpha-D-glucose and fructose
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maltose
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(disaccharide) alpha-1,4 glycosidic linkage btw one alpha-D-glucose and one beta-D-glucose
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cellobiose
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(disaccharide) beta-1,4 glycosidic linkage btw two beta-D-glucose molecules
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starch
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(polysaccharide) storage of glucose in plants, highly water soluble bc poorly branched see slide 60 picture
alpha glycosidic linkages |
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glycogen
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(polysaccharide) storage of glucose in animals, not water soluble bc highly branched see slide 60 picture
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cellulose
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(polysaccharide) very stable, good for structural components see slide 60 picture
beta glycosidic linkages |
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lipids
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nonpolar hydrocarbons
1. fats and oils (energy storage) 2. phospholipids (cell membranes) 3. carotenoids 4. steroids |
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functions
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Fats serve as insulation in animals, lipid nerve coatings act as
electrical insulation, oils and waxes repel water, prevent drying |
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fats and oils....
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monomer: 3 fatty acids and 1 glycerol --> triglyceride (polymer) by ester linkage 3 water molecules see slide 65
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ester linkage
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carboxyl group of fatty acid bonds with hydroxyl group of glycerol forming covalent bond
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saturated fatty acids
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all single bonds btw carbon and hydrogen; packed together tightly - relatively rigid so high melting point (solid at room temp)
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unsaturated fatty acid
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hydrocarbon chain contains one or more double bonds which cause kinks that prevent tight packing
packed together poorly so melting point is low - liquid at room temp |
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phospholipid
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one of the fatty acids of the triglyceride is replaced by a phosphate functional group which acts as the hydrophilic head
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types of lipids
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carotenoids, steriods, vitamins, waxes
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carotenoids
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light-absorbing pigments like beta-carotene which traps light energy in leaves during photosynthesis and is made up of two vitamin A molecules
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steroids
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family of organic compounds whose multiple rings share carbons - used as hormones, c
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vitamins
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small molecules not synthesized by body and must be required by diet
for example, vitamin A is obtained from beta-carotene found in green and yellow vegetables |
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waxes
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highly nonpolar: consists of ester linkage btw a saturated long-chain fatty acid and a saturated long-chain alcohol
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nucleic acids
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two types: DNA, RNA used for storage, transmission, and use of genetic information
polymers of monomeric units nucleotides |
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nucleotides
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consist of pentose sugar, phosphate group, and nitrogen-containing base (either purine or pyrimidine)
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pyrimidine
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single-ringed structure: cytosine, thymine, uracil
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purine
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fused-ring structure: adenine, guanine
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DNA/RNA backbone
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consists of a chain of alternating pentose sugars and phosphate groups (sugar-phosphate-sugar-phosphate) bonded by phosphodiester linkages
phosphate groups link carbon 3' in one pentose sugar to carbon 5' in adjacent sugar |
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DNA
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double-stranded in double helix shape with each strand running in opposite directions in which purines are hydrogen bonded to pyrimidines TA GC
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