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30 Cards in this Set
- Front
- Back
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secondary structure |
the distribution of corkscrews and and zigzags within a protein give a protein this. |
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tertiary structure |
hydrogen bonds and sulfur - sulfur bonds are examples of bonds that fold into a unique and complex three dimensional shape called this |
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quaternary structure |
when two or more polypeptide chains are held together in hydrogen bonds and other non peptide bonds between amino acids int he different chains. example - hemoglobin |
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other macromolecules |
lipoproteins - carry fats glycoproteins- comb. of protein and carbs found on animal cells- helps with immune. |
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shape of a protein molecule determines its function. |
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denaturation- |
disruption of protein folding- like frying and egg |
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enzymes |
the protein shape is critical and they are molecules that initiate and accelerate the chemical reaction in our bodies. |
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active site |
enzymes tertiary or quaternary structure give it a complex shape with lots of nooks and crannies and this is one of those nooks |
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substrate |
provide a safe place for the participants in a chemical reactions and the reactant is... |
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activation energy |
minimum energy or or little push needed to inititate the reaction and its called this |
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metabolism |
all of the chemical reaction in a living organism are its metabolism |
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enzyme and substrate concentration |
for a given amount of substrate an increase in the amount of enzyme increases the rate at which the reaction occurs. it also increases the reaction rate.once all the enzyme molecules are bound to substrate no longer increases the reaction rate. |
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temperature |
because increasing the temperature increases the speed of movement of molecules reaction rates generally increase at higher temperatures. reaction rates continue to increase only up to the optimum temperature for an enzyme. |
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pH |
as with temperature, enzymes have a proper pH, above or below this pH excess hydrogen or hydroxide ions interact with amino acids side chains in the active site.decrease reaction rates. |
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presence of inhibitors |
binding of other chemicals to enzymes. this binding can alter enzyme shape in a way that increases or decreases activity. |
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inhibitors |
reduce enzyme activity and come in 2 types 1. competitive inhibitors and 2. noncompetitive inhibitors |
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competitive inhibitors |
bind to the active site blocking substrate molecules from the site and taking part in the reaction. |
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noncompetitive inhibitors |
do not compete for the active site but rather bind to another part of the enzyme altering its shape in a way that |
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activators |
when it binds to the enzyme it turns it on |
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noble gases |
are more stable because the outer shell is full |
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peptide bond |
is which the amino group of one amino acid is bonded to the carboxl group. |
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dipeptide |
2 amino acids are joined together |
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polypeptide |
several amino acids are joined together. |
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lipoproteins |
circulate in the bloodstream carrying fat |
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glycoproteins |
combo of carbohydrates and proteins |
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nucleic acid |
macromolecule- stores info 2 types 1. deoxyribonucleic acid DNA and 2. Ribonucleic acid RNA |
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nucleotides |
the individual units that make up nucleic acid. 2 components 1. 1 molecule of sugar 2. a phosphate group (contianing phosphorus atom bound to 4 oxygen atoms) 3. and a nitrogen- containing molecule. |
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bases |
attached to each sugar and protruding from the backbone, is one of the nitrogen containing molecules called DNA or RNA bases. - so named because of their chemical structure. |
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double helix |
the two spiraling strands together are said to form a double helix |
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rna |
single stranded |
