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60 Cards in this Set
- Front
- Back
Protein, nucleic acids and carbohydrates are what?
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Polymers
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Polymers are dfined as?
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Long molecules consisting of many similar or identical building blocks linked by covalent bonds
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Most biological polumerizations reactions are?
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condensation (dehydration) reactions
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3 Properties of a condensation reaction
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1) h20 molecule released per polymerization reaction
2)Requires energy 3) Generaly catalyzed by enzymes |
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The break down of a polymer into monomers occurs during what type of reaction
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Hydrolysis reaction
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Properties of a hydrolusis reaction
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1) 1 H2O Molecule consumed per subunit released
2) Catalyzed by enzymes |
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Protein
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organic macromolecule that consists of 1 or more polypeptide chains folded and coiled into a specific functional conformation
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Peptide
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short linear polymer of amino acid subunits linked by peptide bonds
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Polypeptide
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long linear polymer of amino acid subunits linked by peptide bonds
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3 classes of amino acids
(based on side chain |
1 polar
2 nonpolar 3 charged |
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Peptide bond formation is a result of
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Dehydration reactions between amino acids
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the other names for n-terminus and c-teminus
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amino terminus and carboxyl terminus
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Formula for alpha helices
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n-h of amino acid i acts as e donor with carboxyl of i+4
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beta sheets
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adjacent amino acids alternate between amine and carboxyl groups participating in bonds
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primary structure
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arrangement of amino acids in linear form
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secondary structure
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how a single polypeptide twists and pleats due to hydrogen bonds
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tertiary structure
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the polypeptide forms additional hydrogen bonds, van der waals interactions and disulfide bonds with its side-chain and backbone atoms
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quarternary structure
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the interactions between the side chain and backbone atoms of more than one polypeptide in a macromolecule
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The most common exergonic reaction used in coupling is?
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ATP hydrolysis
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Coupling is?
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Using an exergonic reaction to power a endergonic reaction
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1st law of thermodynamics
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Energy cannot be created or destroyed
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2nd law of thermodynamics
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Everytime energy is changed the entropy of the universe
(some energy is lost as heat in biological reactions) |
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ATP hydrolosis
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ATP + H2O --> ADP + Pi
and delta g=-13kcal/mol (of atp hydrolyzed) |
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Enzymes speed up reactions by
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Reducing the energy of activation or Ea
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Transiton state
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unstable condition of reactants that have absorbed enough energy for reaction to proceed
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Enzymes orchestrate which metabolic reactions occur and when by?
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Controlling the concentration of enzymes
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Enzyme cycle
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enzyme + subsrtates(s) -->
enzyme substrates(s) complex--> products +enzyme |
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Active site
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site on the enzyme where the reactions is catalyzed (usually the substrate binding site)
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Binding site
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usually a pocket or groove on the surface of the enzyme with amino acid side chains optimally placed to make specific interactions with the substrate
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Why can a small amount of enzyme catalyze a large amount of the production of a product
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1) Enzyme is unchanged in reaction
2)Weak bonds between enzyme and product can be broken relatively easily |
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Turnover rate
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amount of product produced/an enzyme/second
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How do enzymes lower activation energy
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1) active site may hold 2 reactants in an optimal position for reaction to occur
2)active site atoms can introduce strain into the bonds of the substrates that need to be broken 3) side chain atoms in active site can participate directly in the chemical reaction |
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Enzyme saturation
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When all available active sites are engaged
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irreversible inhibitor
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a substance that selectively (specific enzymes) attaches to an enzyme via covalent bonds and acts as an inhibitor, cannot be sepperated
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Reversible inhibitor
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Inhibitor which connects to an enzyme via weak ineractions. can be removed.
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competitive inhibitor
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a substance which resembles substrate and competes for the binding site
*can be overcome by adding more substrate |
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non-competitive inhibitor
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a substance which binds to an area of the enzyme which is not the active site
*cannot be overcome by adding more substrate |
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cofactor
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substance which helps enzyme catalyze a reaction eg. vitamins or Mg2+
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Allosteric regulation
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regulator molecule binds at allosteric site and shifts equilibrium toward active or inactive conformation
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Allosteric activator
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molecule that shifts equilibrium toward active conformation
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Allosteric inhibitor
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molecule that shifts equilibrium toward inactive conformation
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feedback inhibition
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down-regulation of a metabolic pathway by its end product via the inhibition of an enzyme that catalyzes and early reactions in the pathway
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enzyme cooperativity
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binding of substrate to one active site increases the binding of additional substrates to additional active sites in the enzyme
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nucleic acid
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polymer of nucleotide monomers linked via phosphodiester linkages
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2 types of nucleic acid
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ribonucleic acid RNA
deoxyribonucleic acid DNA |
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Nucleotide consts of what 3 parts?
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-5 carbon sugar
-phosphate group -nitrogenous base |
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Which Carbon is the phosphate attached to?
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5'
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Which carbon is the nitrogenous base attached to?
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1'
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pyrimidines
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6 membered ring
3 kinds: cytosine-c-both dna rna thymine-t-dna only uracil-u-rna only |
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purines
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double ring structure
guanosine-g-both dna rna adenine-a-both dna rna |
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Phosphodiester linkage
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connects two nucleotides by connecting the 3' carbon of nucleotide "n" with the 5' carbon of nucleotide 'n+1"
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Two end of linear polymer
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begins at 5' end
ends at 3' end |
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how does dna sequence determine protein sequence
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dna-------->rna--------->protein transcription translation
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pyrimidines
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6 membered ring
3 kinds: cytosine-c-both dna rna thymine-t-dna only uracil-u-rna only |
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purines
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double ring structure
guanosine-g-both dna rna adenine-a-both dna rna |
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Phosphodiester linkage
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connects two nucleotides by connecting the 3' carbon of nucleotide "n" with the 5' carbon of nucleotide 'n+1"
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Two end of linear polymer
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begins at 5' end
ends at 3' end |
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how does dna sequence determine protein sequence
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dna-------->rna--------->protein transcription translation
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what is a codon
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a set of 3 nitrogenous bases in DNA/RNA
64 possible codons (4^3) for 20 amino acids |
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Ribosome
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enzyme that catalyzes synthesis of polypeptide is
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