bio vocab 3
Terms
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- allosteric regulation
- the binding of a molecule to a protein that affects the function of the protein at a different site
- saturation kinetics
- effect of various factors; study of rates; how fast does an enzyme work under different conditions
- active site
- the place on an enzyme where the substrate binds
- dehydration reaction
- removes water molecule forming a new bond in the synthesis of a polymer
- cilium
- a short cellular appendage specialized for locomotion, formed from a core of nine outer doublet microtubules and two inner single microtubules enheathed in an extension of plasma membrane
- primary structure (of protein)
- linear sequence of amino acids in a protein
- cytoskeleton
- proteinaceous network throughout cytoplasm involved in cell shape and movement; consists of at least three rod like or fiber like elements ( microtubules, microfilaments, intermediate filaments), can assemble rapidly, disassemle. throughout the cytoplasm and a variety of mechanical and transport functions
- polymer
- molecule consisting of identical of similar subunits linked together end to end
- transition state
- bonds are being broken and others are being formed
- quaternary structure
- interactions between two or more polypeptides creating a functional protein; coded by genes and amino acids; three dimensional arrangement
- alpha-helix
- looks like a slinky; one form of the secondary structure of proteins arising from a specific hydrogen bonding structure
- enzyme
- allow reactions to happen without additional heat
- peptide bond
- covalent bonds between amino acids; connect the amino nirtogen of one monomer witht he carboxyl carbon of the next; the result of dehydration reactions
- free energy
- the portion of a systems energy available to do work; less is more stability and less capacity to do work
- polypeptide
- a polymer consisting of many amino acids linked together by peptide bonds
- intermediate filament
- 8-12 nm protein-variable, very little dynamic properties, lead to stability rather than change, reinforce cell shape and fix organelles in position
- noncompetitive inhibitor
- a substance that reduces the activity of an enzyme by binding to a location remote from the active site, changing its conformation so that it no longer binds to the substrate
- amino acid
- an organic molecule possessing both carboxyl and amino groups; serve as the monomers of proteins
- centrosome
- material present in the cytoplasm of all eukaryotic cells, important in cell division; the microtubule organizing center
- endergonic
- anabolic, not spontaneous, unfavorable, energy requiring, uphill
- peptide backbone
- regular structure that forms when amino acids link together through making an amide bond
- feedback inhibition
- a methood of metabolic control in which the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway; an allosteric strategy used by cells to regulate metabolic pathways; the end product of a pathway is an allosteric inhibitor of an early reaction in the pathway
- enzyme substrate complex
- a temporary complex formed when an enzyme binds to its substrate molescules
- centriole
- a structure in an animal cell composed of cylinder of microtubule triplets arranged in a 9 + 0 pattern. an animal cell usually has a pair of centrioles involved in cell division
- induced fit
- the change in shape of the active site of an enzyme so that it binds more snugly to the substrate, induced by entry of the substrate
- catabolism
- breaks down complex molecules to simpler ones; releases energy
- coenzyme
- an organic molecule serving as a cofactor. most vitamins function as coenzymes in important metabolic reactions
- anabolism
- builds large molecules from simple ones; requires energy
- secondary structure
- regular coiling or folding of an amino acid chain due to hydrogen bonding within the polypeptide backbone
- chaperonin
- a protein molecule that assists the proper folding of other proteins
- tertiary structure
- irregular twisting and looping of the primary and secondary structure due to interactions among the side chain; this level gives each individual polypeptide its overall shape; hydrophobic and hydrogen bond interactions stabilize tertiary structure
- denaturation
- in proteins, a process in which a protein unravels and loses it native conformation, thereby becoming biologically inactive. Occurs under exteme conditions
- tubulin
- protein found in microtubules,
- microtubule
- 25nm, protein-tubulin, dynamic(can change length and action)
- motor protein
- powered by ATP, proteins are located on an organelle or cytoskeletal element; walk along another cytoskeletal element by changing shape
- monomer
- subunit that serves as the building block of a polymer
- flagellum
- long cellular appendage specialized for locomotion
- hydrolysis
- polymers are broken down by adding water to a molecule
- beta-pleated sheet
- one form of the secondary structure of proteins in which the poly peptide chain folds back and forth. Two regions of the chain lie parallel to each other and are held together by hydrogen bonds
- catalyst
- a chemical agent that changes the rate of a rection without being consumed by the reaction
- microvillus
- contain actin, increase surface of cell, in small intestine
- basal body
- extension of microtubules into the cell
- competitive inhibitor
- a substance that reduces the activity of an enzyme by entering the active site in place o the substrate whose stryctyre it mimics
- metabolism
- the total of all the chemical activity in a call or organism
- substrate
- the reactant on which an enzyme acts, converting it to products
- macromolecule
- made in living systems from smaller building blocks covalently bonded; four classes: proteins, nucleic acids, carbohydrates, and lipids
- exergonic
- classification of chemical reactions; catabolic, stpontaneous, favorable, energy yielding, downhill
- actin
- protein found in microfilaments, muscle and other contractile elements
- disulfide bridge
- formed by reactions between sulfhydryl groups in two cystine amino acids; a strong covalent bond formed when the sulfer of one cystine monomer bonds to the sulfer of another cysteine monomer
- cooperativity
- an interaction of the constituent subunits of a protein whereby a conformational change in one subunit is transmitted to all the others
- activation energy
- the amount of energy that reactants must absorb before a chemical reaction will start
- cofactor
- any nonprotein molecule or ion that is required for the proper functioning of an enzyme. can be permanently bound to the active site or may bind loosely with the substrate during catalysis
- metabolic pathway
- a group of enzymes that cooperate to accomplish some task; versatility is a major benefit because of branching
- microfilament
- 7nm, protein-actin, dynamic (can change length and action)