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33 Cards in this Set
- Front
- Back
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Protein monomer
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amino acids
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Carbohydrate monomer
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simple sugars (glucose, fructose)
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Lipid monomer
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glycerol and fatty acids
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nucleic acid monomer
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nucleotides
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amino acid structure
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amino group (NH2), carboxyl group (COOH), R group sometimes with sulfhydryl (-SH) attachment
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zwitterions
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monomeric amino acids used as Ph buffers through dehydration synthesis
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Primary Structure
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linear order of amino acid chain, dictates secondary and tertiary structure
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Secondary Structure
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alpha-helix or beta-pleated sheets
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Tertiary Structure
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bonding and interactions between side chains farther apart than those in secondary structure. Such as disulfide bridges, bunching of hydrophilic AA
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Quaternary Structure
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multi-subunit structure formed with other proteins, exhibits properties no subunits exhibit alone.
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Saturated Fatty Acid
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only single bonds within hydrocarbon chain
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Unsaturated Fatty Acid
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on or more double bonds within hydrocarbon chain. Create "kinks"
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Fatty Acid Chemical Formula
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CH3(CH2)nCOOH
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Esterfication sites
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sites where glycerol binds to fatty acid chains
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Phospholipids
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predominant class of lipid in cell membrane. contains glycerol+2 fatty acid chains+a phosphate group attached to a variable R group
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Emulsification
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amphipathic lipids surround a fat droplet and break it into smaller particles
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chylomicrons
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lipid complexes that surround and transport fats from the intestine to other tissues.
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Steroids
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non-glyceride lipids. characterized by common core of four rings
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sphingolipids
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other group of non-glyceride lipids
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glycosidic bonds
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joins carbohydrates together
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alpha linkage
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glycosidic bonds resulting in kinks resulting in twisty and branching configuration (glycogen or starch)
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beta linkage
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glycosidic bonds which allow for the formation of straight chains of sugar (cellulose)
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chitin
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amino-sugar that builds hard exoskeletons of insects and crustaceans
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nucleotide structure
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phosphate group+sugar group+nitrogenous base
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substrate molecules
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particular molecule an enzyme binds to
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kinetics
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rate of reaction. this is what enzymes effect
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Vmax
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maximum reaction rate. Occurs when enzymes become saturated.
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Lock-and-key model
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spatial structure of enzyme's active site complimentary to substrate
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Induced Fit
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enzyme active site flexible, shifts to accommodate incoming substrate
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transition state
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state in an enzymatic reaction where substrate is neither original substrate molecule or product
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Feedback Inhibition
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Enzyme product blocks original enzymes that start reaction
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Competitive Inhibition
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Certain molecules compete with substrate for enzyme's reaction site
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Allosterically
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way substances control enzymes by binding to sites other than active sites and decrease efficiency of enzyme (hemoglobin)
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