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unit one ap bio

QuestionAnswer
four elements that make up 96% of living matter oxygen, carbon, hydrogen, nitrogen
atomic structure composed of protons, neutrons, and electrons (2,8,8)
reactivity of atoms controlled by the number of electrons in an atom; fuller shell is more stable
nonpolar covalent bonds equal sharing of electrons
polar covalent bonds unequal sharing of electrons
covalent bonding results from the sharing of electron pairs between two atoms
ionic bonding transfer of electrons between a metal and a non-metal (held by charge differences)
polarity of water water is a polar molecule meaning it has opposite charges on opposite ends. this causes hydrogen bonds to form causing water to stick together
hydrogen bonding forms when a hydrogen atom covalently bonded to one electronegative atom is also attracted to another electronegative atom
four emergent properties of water universal solvent cohesion/adhesion, moderation of temperature, floating of ice in liquid water,
cohesion the sticking together of particles of the same substance (wax + water)
adhesion force of attraction between different kinds of molecules (table + water)
hydrophilic water loving
hydrophobic water fearing
surface tension a measure of how hard it is to break the surface of a liquid
hydrogen bonds break heat is absorbed
hydrogen bonds form heat is released
moderation of temperature water absorbs heat from warmer air and releases stored heat to cooler air
water's high specific heat heat required to raise or lower the temperature of 1 gram of an object 1 degree C; keeps earth ocean temps stable
evaportaive cooling allows water to cool a surface
solute the substance that is dissolved
solvent the "dissolver"; water is the universal solvent
pH scale 0-6 acidic 0-6 acidic 7 neutral 8-14 basic
acids hydronium ions (H+ or H3O+)
bases hydroxide ions (OH-)
changes in pH concentrations can have effect a great affect on pH in living organisms
buffers substances that minimize changes in pH
orgainic chemistry the study of carbon atoms
Miller-Urey Experiment proved that abiotic compounds can turn into biotic compounds
carbon is unparalleled in its ability to form large, complex, and diverse molecules carbs, proteins, lipids, nucleic acids (DNA)
carbon skeleton can be chains, ring-shaped, or branched; may vary in length and shape
structural isomer varies in covalent arrangement
cis-trans isomer differs in spatial arrangement
enantiomers mirror image of molecules
hydroxl group OH-; alcohols
carboxyl group -COOH; carboxylic acid (organic acid)
amino group -NH2; amines, acts as a base
phosphate PO4 3-; organic phosphates
macromolecules giant molecules; 2 or more polymers bonded together
carbohydrates used for energy
fats or lipids storing energy, protection of vital organs and insulation
proteins help repair and build body tissue
nucleic acids storage and expression of genomic information
monomers building blocks of polymers (dehydration synthesis)
polymers large compound formed from combinations of many monomers (covalent bonds)
dehydration synthesis makes polymers; A +B --> AB
hydrolysis breakdown polymers; AB --> A + B
monosaccharides simple sugars; glucose, fructose, galactose
disacchaides complex sugars; sucrose, lactose, maltose
polysaccharides complex sugars; starch, cellulose, glycogen
glycosidic linkage a covalent bond formed between 2 monosaccharides by a dehydration reaction
starch stores sugar in plants, made up of alpha-glucose molecules
cellulose made up of ß-glucose molecules
glycogen stores sugar in animals
chitin structural molecule in walls of fungi/arthropod exoskeletons
lipid structure composed of 3 fatty acids and 1 glycerol molecule (triglyceride)
saturated fats fats that are solid at room temperature (butter)
unsaturated fats liquid at room temperature (oils)
phospholipids a lipid consisting of a glycerol bound to two fatty acids and a phosphate group
cholesterol a component of the plasma membranes in animal cells; keeps the membranes flexible and fluid
amino acid structure central carbon, amino group, carboxyl group, R group, hydrogen atom
polypeptides chains of amino acids
protein contains one or more polypeptides
primary structure sequence of amino acids; peptide bonds
secondary structure forms a coil; hydrogen bonds
tertiary structure bonds between R groups; hydrogen bonds, ionic bonds, disulfide bonds, van der waals interactions
quaternary bonds two or more peptide bonds
protein function the shape determines how it functions
denaturation of proteins temperature, pH, solvents that disrupt ionic, hydrogen, or hydrophobic interactions
nucleotide structure phosphate, sugar, base
DNA double stranded deoxyribose sugar stores and transmits genetic information AGCI
RNA single stranded ribose sugar carry info from DNA to ribsomes AGCU
DNA bases A-T G-C
RNA bases A-U G-C
metabolism the chemical processes that occur within a living organism in order to maintain life
catabolic breaking down
anabolic building up
kinetic energy energy of motion
potential energy stored energy
chemical energy energy stored in chemical bonds
1st law of thermodynamics energy cannot be created nor destroyed
2nd law of thermodynamics cells require a constant input of energy
free energy used to determine how systems change and how much work they can produce
endergonic absorbs energy; builds up
exergonic releases energy; breaks down
ATP like a charged battery (adenine, ribose, 3 phosphates)
ADP like a dead battery (ribose, adenine, two phosphate groups)
energy coupling occurs when the energy produced by one reaction or system is used to drive another reaction or system
enzyme protein that acts as a biological catalyst
catalyst substances that can change the rate of a reaction without being alerted in the process
activiation energy the minimum amount of energy required to start a chemical reaction
active site a region on an enzyme that binds to a protein or other substance during a reaction
substrate chemcial that an enzyme works on
enzyme-substrate complex a temporary complex formed when an enzyme binds to its substrate molecule(s)
products the substances that are formed by the chemical change
factors that affect enzyme activity temperature, pH, chemicals
cofactors nonprotein enzyme helpers
coenzymes organic cofactors
competitive inhibitor binds to the active site of an enzyme, competes with substrate
noncompetitive inhibitor binds to another part of an enzyme --> enzyme changes shape --> active site is nonfunctional
activator stabilizes active site (turns on)
inhibitor stabilizes inactive form (turns off)
allosteric regulators substances that can either inhibit or activate enzymes
feedback inhibition the end product of the enzymatic passages - cells regulate how products are made
Created by: helaraky16
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