Biochemistry

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Last updated 7:34 PM on 1/15/23
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51 Terms

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Active site
________:: part of enzyme that binds to the structure to form the product and help with the reaction.
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Hydrolysis
________:: adding water to break bonds of polymers, results in monomers.
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Adhesion
________:: water sticks to something else (but not nonpolar substances), allows transpiration in plants.
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Buffers
________:: resist sharp changes in pH in aqueous solutions, acids and bases neutralize each other.
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Dehydration synthesis
________:: remove water to join monomers to form new molecules.
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Catalyst
________:: increases rate of a chemical reactions without changing itself.
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Polar covalent
________:: valence electrons are unequally shared.
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straight hydrocarbon
Saturated fatty acid:: lack double bonds, ________ chains, help hormone production and protein signaling, solid at room temp.
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high surface
Cohesion:: water sticks to itself, ________ tension, also helps transport water in plants.
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Catabolic pathway
________:: break molecules into smaller units, release energy.
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Polymer
________:: substance made of smaller, simpler monomers.
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Anabolic pathway
________:: build complex molecules from simpler ones, need an input of energy.
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Quaternary structure
________:: coil of tertiaries, most affected by denaturation.
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Competitive inhibition
________:: substance with similar shape to substrate binds to and blocks active site.
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High specific heat
________:: water absorbs a lot of energy before its temperature changes, prevents sudden rise in temp in living organisms.
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Molecular diversity
________:: can form 4 chemical bonds to other atoms, small size fits into many large molecules.
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Hydrogen bond
________:: weak bond between hydrogen and N, O, or F; results from polarity and electronegativity, occurs between molecules.
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nonpolar covalent
Hydrophobic:: caused by ________ bonds and hydrophobic fatty acid tails, mostly nonpolar C- H bonds.
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Monomer
________:: molecule that can be bonded to other identical molecules to form a polymer.
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polar covalent
valence electrons are unequally shared
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nonpolar covalent
valence electrons shared equally
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ionic
transfer of electrons, forms an anion and cation
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hydrogen bond
weak bond between hydrogen and N, O, or F; results from polarity and electronegativity, occurs between molecules
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adhesion
water sticks to something else (but not nonpolar substances), allows transpiration in plants
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cohesion
water sticks to itself, high surface tension, also helps transport water in plants
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high specific heat
water absorbs a lot of energy before its temperature changes, prevents sudden rise in temp in living organisms
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acids
dissociate in water, release hydrogen ions
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bases
either take up hydrogen ions (H+) or release hydroxide ions (OH-), proton acceptor
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buffers
resist sharp changes in pH in aqueous solutions, acids and bases neutralize each other
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structural
same formula, different order
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cis trans
same formula, different positioning around double bond
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enantiomers
same formula, mirror image positioning
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hydrolysis
adding water to break bonds of polymers, results in monomers
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dehydration synthesis
remove water to join monomers to form new molecules
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saturated fatty acid
lack double bonds, straight hydrocarbon chains, help hormone production and protein signaling, solid at room temp
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unsaturated fatty acid
hydrocarbon chain, at least one double bond covalent bond, ends in carboxyl group
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hydrophobic
caused by nonpolar covalent bonds and hydrophobic fatty acid tails, mostly nonpolar C-H bonds
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primary structure
linear amino acids (monomer), least denaturation when temp changes
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secondary structure
alpha helix or b-pleated sheet
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tertiary structure
most functional, random coil, S-S bonds, interacting R groups
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quaternary structure
coil of tertiaries, most affected by denaturation
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endergonic reaction
energy absorbed, reaction isnt spontaneous, requires energy to be driven
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exergonic reaction
energy released, reaction is spontaneous
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anabolic pathway
build complex molecules from simpler ones, need an input of energy
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catabolic pathway
break molecules into smaller units, release energy
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catalyst
increases rate of a chemical reactions without changing itself
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active site
part of enzyme that binds to the structure to form the product and help with the reaction
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induced fit
enzyme causes change in shape of substrate, contrasts lock and key fit
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competitive inhibition
substance with similar shape to substrate binds to and blocks active site
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noncompetitive inhibition
molecules bind to another part of the enzyme, changing its shape and function
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feedback inhibition
enzyme is inhibited by the substrates end product after interacting with the enzyme