Biochemistry Unit 1 AP Biology Full – Flashcards
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ionic bond
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bond resulting from a transfer of electrons (electrons being ripped off)
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covalent bond
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bond resulting from the sharing of electrons
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nonpolar
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electrons shared equally
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polar covalent bond
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bond resulting from electrons shared unequally
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buffer
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substance that resists changes in pH
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bicarbonate ion
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most important buffer in human blood
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isomer
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organic compounds with the same molecular formula but different structure
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monosaccharide
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C6H12O6 simple sugar; glucose, galactose, and fructose
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disaccharide
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two monosaccharides joined together; C12H22O1; maltose, lactose, and sucrose
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dehydration synthesis
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condensation; joining compounds together with water released
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hydrolysis
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breakdown of a compound by adding water
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polysaccharide
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polymers of carbohydrates ("many" sugars)
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cellulose
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structural polysaccharide that makes up plant cell walls
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starch
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storage polysaccharide found in plants
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amylose
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simplest storage polysaccharide form of starch
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amylopectin
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more complex storage polysaccharide form of starch
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chitin
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structural polysaccharide found in animals; makes up the exoskeleton in arthropods
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glycogen
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storage polysaccharide animal starch that in humans is stored in the liver and the skeletal muscle
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glycerol
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alcohol portion of a lipid
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fatty acid
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hydrocarbon chain with a carboxyl group at one end; attaches to glycerol
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saturated fat
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fat without double bonds
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unsaturated fat
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fat with double bonds
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steroid
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lipid with a four fused ring structure; cholesterol and testosterone
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peptide bond
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bond creating amino acid chains or polymers (bond between amino acids)
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conformation
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protein's unique shape that determines its function
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primary structure
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linear sequence of amino acids; peptide bonds
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secondary structure
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protein formed with hydrogen bonds
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tertiary structure
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3D conformation formed; determines specificity, due to hydrogen bonds, disulfide bridges, hydrophobic interactions and ionic bonds
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quaternary structure
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protein with more than one polypeptide chain
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alpha helix
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secondary structure form of a protein; human hair (keratin)
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beta pleated sheet
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secondary structure form of a protein; spider webs and silk
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heme group
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one of four polypeptide chains in the quaternary structure of hemoglobin
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protein folding problem
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how proteins form their unique shapes
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functional group
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components of organic molecules most often involved in chemical reactions
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metabolism
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sum of all chemical reactions that take place in cell
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enzyme
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catalytic protein that lowers a reaction's energy of activation
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induced fit model
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enzyme model where the substrate induces the enzyme to alter its shape slightly so it fits better
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cofactor
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inorganic enzyme assist
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coenzyme
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organic enzyme assist (vitamins)
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competitive inhibition
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compounds that look like the normal substrate compete for the same active site on the enzyme
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noncompetitive inhibition
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more than one active site and the substrates do not look like each other
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allosteric inhibition
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two active sites, one for a substrate and one for an inhibitor
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feedback inhibition
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metabolic pathway is switched off by the end product; allosteric inhibition
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cooperativity
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substrate stimulating an enzyme with quaternary structure to be more effective
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cohesion
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like molecules sticking together
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alkaline
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synonym for basic
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salt
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compound that releases ion other than H+ or OH- when dissolved in water
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chemical equilibrium
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when the reaction rate is about the same in either direction
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polymer
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long molecule consisting of many similar or identical monomers linked together
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monomer
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building block for polymers; only made by producers
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adhesion
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attraction between different kinds of molecules
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surface tension
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measure of how difficult it is to stretch or break the surface of a liquid
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van der Waals interactions
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tertiary structure; weak attractions between molecules or parts of molecules that result from localized charge fluctuations
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evaporative cooling
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property of a liquid where the surface becomes cooler during evaporation due to the loss of molecules
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hydration shell
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sphere of water molecules around each dissolved ion
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disulfide bridge
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tertiary structure; strong covalent bond formed when one sulfur of one cysteine monomer bonds to the sulfur of another
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hydrophobic interaction
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tertiary structure; weak chemical bond formed when molecules that do not mix with water change to exclude the water
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hydrocarbon
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organic molecule consisting of only hydrogen and carbon
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macromolecule
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giant molecule formed by the joining of smaller molecules
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glycosodic linkage
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covalent bond formed between two monosaccharides by a dehydration synthesis reaction
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triose
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three carbon sugar
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pentose
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five carbon sugar
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hexose
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six carbon sugar
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hydroxyl
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hydrogen bonded to oxygen bonded to an organic molecule's carbon skeleton; alcohol; polar
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carboxyl
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oxygen double bonded to a carbon atom that is bonded to a hydroxyl group
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amine
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nitrogen bonded to two hydrogens and to the carbon skeleton
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phosphate
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phosphorous bonded to four oxygens, two have negative charges, one is bonded to the carbon skeleton; phospholipid
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isotope
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atoms with same number of protons but different number of neutrons
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hydrogen bond
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weak bond between hydrogen and a highly electronegative atom like nitrogen or oxygen
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acid
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more H+ than OH- ions, pH below 7
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base
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more OH- than H+ ions, pH above 7
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pH
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measure of H+ ions in a solution
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triglyceride
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glycerol plus 3 fatty acids
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phospholipid
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has a hydrophilic head and hydrophobic tail, major component of cell membrane
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LDL
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low density lipoprotein, "bad cholesterol"
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HDL
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high density lipoprotein, "good cholesterol"
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amino acid
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contain carboxyl group (COOH) and amino group (NH2) and side chain R.... make up proteins
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chaperonin
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a protein that assists in the proper folding of a polypeptide into a protein
