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94 Cards in this Set

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WATER
most abundant molecule in cells at 70% of the cell mass
CYTOSOL
aqueous component of the cytoplasm that does not contain organelles
HYDROLYSIS
1. chemical decomposition of macromolecules, disassembly of polymers into monomers by reacting with water
2. opposite of dyhydration reactions
DEHYDRATION/CONDENSATION
1.covalent bonding of monomers through the loss of a water molecule that requires energy and enzymes
2. opposite of hydrolysis reactions
MACROMOLECULES
nutrients in their unbroken down state; polymers consisting of repeating subunits (40-50 monomers)
INTERMOLECULAR BONDS
forces of attraction BETWEEN the molecules of a substance or substances; weaker than covalent or ionic bonding
HYDROGEN BONDS
intermolecular force between two partial electric charges of opposite polarity, like two water molecules or between the NH and CO groups of the peptide backbone, create tertiary and secondary structures
HYDROPHILIC
water loving or polar molecules
HYDROPHOBIC
water fearing or non-polar molecules
POLAR MOLECLUES
molecules that have a slightly positive part and a slightly negative part
AMPHIPATHIC
molecule contains both hydrophobic/non-polar and hydrophilic/polar groups
LOW SOLUBILITY
incapable of being dissolved; insoluble
TERPENES
major group of lipids made up of hydrocarbons
TRIGLYCERIDES
major group of lipids; three carbon chains dangling from a three carbon backbone and each carbon chain attached by an ester group
FATTY ACIDS
major group of lipids; amphiapathic consisting of a carboxylic acid and carbon chain; either saturated or unsaturated
SATURATED FATTY ACIDS
all carbons in the chain are connected by single bonds, thus fully saturated with hydrogen atoms
UNSATURATED FATTY ACIDS
the carbon chain has at least one double bond; lower melting point
PHOSPHOLIPIDS
major group of lipids; consists of three carbon backbone, two carbon chains attached to the backbone by an ester group, third backbone carbon has a phosphate group attached; amphipathic molecule
LIPID BI-LAYER
composed of phospholipid molecules found in cell membranes; polar regions face aqueous solution inside and outside the cell; non-polar carbon chains face the interior of the membrane
GLYCOLIPIDS
are like phospholipids but phosphate group is replaced with a carbohydrate
STERIODS
major group of lipids, four ring structures slightly amphiapathic
LIPOPROTEINS
particles (not molecules) comprised of proteins and lipids shell that surrounds lipids for transport
PROTEINS
organic compounds made up of long chains of amino acids
AMINO ACIDS
molecule that contains both amine and carboxylic acid functional groups, plus a side chain attached to the α–carbon; 20 types of amino acids
ALPHA CARBON
the first carbon attached to the carbonyl carbon and an amine; stereocenter for every amino acid except glycine
SIDE CHAIN
one of 20 possible structures that distinguish the 20 common amino acids; placed in four categories polar, non-polar, basic and acidic
ESSENTIAL AMINO ACID
between 8-11 amino acids that the body cannot produce in sufficient quantities and are to be provided via diet
PRIMARY STRUCTURE OF PROTEIN
number and sequence of amino acids including the locations of the disulfide bonds between cysteines
SECONDARY STRUCTURE OF PROTEIN
generated by the twisting of the α-helix or the folding of the β-pleated sheets, held together by hydrogen bonds between the amine of one amino acid residue and the carbonyl oxygen of another residue
TERTIARY STRUCTURE OF PROTEIN
the bending of the amino acid string into a pretzel shape or a glob via five forces hydrogen bonds, covalent disulfide bonds, ionic bonds, hydrophobic and hydrophilic effects and electrostatic forces/Van der Waals
QUATERNARY STRUCTURE OF PROTEIN
consists of two or more of these pretzel-like polypeptides held together by the same five forces that hold together the tertiary structure
PEPTIDE
small number of amino acids are joined together to form a protein by peptide bonds
PEPTIDE BOND
formed between amino acids when the carboxyl group of one molecule reacts with the amino group of the other releasing a molecule of water (H2O)dehydration synthesis reaction, resulting in a CO-NH bond and amide molecule
POLYPEPTIDE
long chain of amino acids joined together to form a protein by a series of peptide bonds
AMINO ACID RESIDUE
an amino acid incorporated into the peptide chain
GLOBULAR PROTEINS
protein with tertiary and quaternary structure
BETA-PLEATED SHEETS
polypeptide chain can be extended into a sheet-like structure by hydrogen bonding with another chain that runs in the same or opposite direction, hydrogen bonding involves the C=O group of one peptide bond and the NH group of another
ALPHA HELIX
righthanded coiled conformation stabilized by hydrogen bonds formed between the C=O group and NH group of the peptide bond four residues farther along the polypeptide chain, one turn for every 4 amino acids
DISULFIDE BOND/DISULFIDE BRIDGE
S-S BOND is a single covalent bond between two cysteines that are themselves not bonded to sulfur
IONIC BONDING
occur between amino acids with oppositely charged groups like acidic and basic amino acids
HYDROPHILIC AND HYDROPHOBIC EFFECTS
occur between amino acids with the same polar and nonpolar side chains
ELECTROSTATIC FORCES
the forces between particles that are caused by their electric charges
VAN DER WAALS FORCES
where portions of the molecule have dipoles or instantaneous dipoles
PROTEIN SUBUNIT
single protein molecule that assembles with other protein molecules to form a quaternary structure
DENATURIZATION
addding heat or chemicals to disrupt the five forces, primary structure exempt, resulting in the unfolding of polypeptide chain
GLYCOPROTEINS
proteins with carbohydrate portions attached
PROTEOGLYCANS
carbohydrates with protein portions attached
CYTOCHROMES
proteins that require non-proteinaceous portions to function; embedded in the inner membrane of the mitochondrion and pass down high energy electrons from one protein to the next
CONJUGATED PROTEINS
proteins with non-proteinaceous groups
CARBOHYDRATES
consists of carbon and water Cn(H2O)n, water is added to break of individual glucose molecules
GLUCOSE
most important carbohydrate monosaccharide used as a source of metabolic energy, made up of an aldehyde with four chiral carbons C6H12O6
BETA ANOMER
stereoisomer of the cyclic form of a carbohydrate in which the hydroxyl group at C-1 is UP
ALPHA ANOMER
stereoisomer of the cyclic form of a carbohydrate in which the hydroxyl group at C-1 is DOWN
GLYCOGEN
carbohydrate chains of glucose molecules attached via alpha-linkages stored in animals
STARCH
chief form of fuel storage in most plants that contain alpha-linkages and resembles glycogen
CELLULOSE
plant cell walls are made from this carbohydrate chain, glucose molecules attached via beta-linkages
NUCLEOTIDES
made up of ribose sugar, nitrogenous base, and phosphate group; they are the structural units of DNA and RNA
NUCLEIC ACID
complex, high-molecular-weight biochemical macromolecule composed of nucleotide chains that convey genetic information like DNA and RNA
DNA
deoxyribonucleic acid; double stranded helix containing the genetic instructions monitoring the biological development of all cellular forms of life
RNA
ribonucleic acid; single-stranded molecules transcribed from DNA containing along the strand a linear sequence of nucleotide bases that is complementary to the DNA strand from which it is transcribed
NADH
important nucleotide in the reduced form of nicotinamide adenine dinucleotide (NAD) in electron transport reactions
FADH
important nucleotide in the reduced form of flavin adenine dinucleotide (FAD)functions in certain oxidation-reduction reactions in the body
ATP
adenosine triphosphate; supplies large amounts of energy to cells for various biochemical processes, including muscle contraction and sugar metabolism, through its hydrolysis to ADP
cyclic AMP
cyclic nucleotide of adenosine that acts at the cellular level to regulate various metabolic processes and mediate the effects of many hormones
MINERALS
inorganic elements that exist in the form of ions inside and outside the cell; establish electrochemical gradients, act as co-factors to enable protein function, and form matrix compounds in bone and else where
ENZYMES
catalyst and protein that increases the reaction rate by lowering activation energy, one enzyme for nearly every reaction in a living cell
ACTIVATION ENERGY
energy needed to break the bonds of the reactants creating the transition state or the species between the reactants and the products
CATALYST
substance that initiates or accelerates a chemical reaction without itself being affected, example being the function of enzymes to break down organic matter
TRANSITION STATE
the activated state of a molecule that has partly undergone a chemical reaction
SUBSTRATE
molecule or molecules an enzyme works on, they attach to the enzymes at an active site which may fit like a key in a lock or induce the enzyme to change shape to make it fit
LOCK AND KEY MODEL
when only a certain substrate (key) can fit into a certain active site (key hole) in the enzyme (lock)
INDUCE FIT MODEL
moulds enzyme to change shape to make substrate fit it
ENZYME SPECIFICITY
each enzyme must be tailored made for one reaction, which gives the cell more control in regulating chemical reactions
SATURATION KINETICS
occurs after the substrate has bound to the enzyme no further rate increase is possible even after adding more substrate
OPTIMAL TEMPERATURE
enzymes are dependent upon a temperature until it denatures (enzymes are proteins)
OPTIMAL pH
enzymes are dependent upon a narrow pH range (near neutrality) and will denature when pH is too far
FEEDBACK INHIBITION
works at the protein level and occurs when a product of a reaction near the end of a chain of reactions inhibits the function of an enzyme of an earlier reaction in that chain
COMPETITIVE INHIBITION
where binding of the inhibitor to the enzyme prevents binding of the substrate and vice versa, can be overcome by high substrate concentrations
NON-COMPETITIVE INHIBITION
does not attach to the active site instead it changes the shape of the enzyme so the substrate doesn’t fit as well, cannot be overcome with substrate concentration
IRREVERSIBLE INHIBITION
combine with the enzyme by forming a strong, covalent bond
ZYMOGEN/PROENZYME
an inactive enzyme precursor that requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme
PHOSPHORYLATION
the addition of a phosphate (PO4) group to a protein or a small molecule or the introduction of a phosphate group into an organic molecule
DEPHOSPHORYLATION
subtraction of a phosphate (PO4) group to a protein or a small molecule or the introduction of a phosphate group into an organic molecule
CONTROL PROTEINS
activate or inactivate enzymes
CELLULAR RESPIRATION
metabolic processes where certain organisms obtain energy from organic moelcules; processes that take place in the cells and tissues during which energy is released and carbon dioxide is produced and absorbed by the blood to be transported to the lungs
METABOLISM
the sum of the physical and chemical processes in an organism by which its material substance is produced, maintained, and destroyed, and by which energy is made available
GLYCOLYSIS
conversion of a monosaccharide (generally glucose) to 2 pyruvates that produces 2 ATPs, and 2 NADHs via the glycolytic pathway in the cytosol
AEROBIC RESPIRATION
the release of energy from glucose or another organic substrate in the presence of Oxygen; oxidation or combustion of glucose
ANAEROBIC RESPIRATION
the release of energy from glucose or another organic substrate in the absence of Oxygen
FERMENTATION
energy-yielding anaerobic metabolic breakdown of a nutrient molecule, like glucose, that yields lactic acid, carbon dioxide, ethanol, or some other simple product
MITOCHONDRION
rod-like structures inside cells of the body whose primary functions include the production and regulation of energy for all cellular functions
ELECTRON TRANSPORT CHAIN
group of electron carriers in mitochondria that transport electrons to and from each other in a sequence, in order to generate ATP
KREBS CYCLE/CITRIC ACID CYCLE
series of reactions by which fragments from any of the energy nutrients (proteins, carbohydrates, and fats) are completely broken down to carbon dioxide and water, releasing energy for the formation of adenosine triphosphate (ATP), the final common pathway for all nutrient metabolites involved in energy production, and provides more than 90% of the body's energy
ATP SYNTHASE
enzyme in mitochondria's nucleus that produces ATP by adding a phosphate group to the molecule ADP by utilizing some form of energy