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60 Cards in this Set

  • Front
  • Back
Protein, nucleic acids and carbohydrates are what?
Polymers
Polymers are dfined as?
Long molecules consisting of many similar or identical building blocks linked by covalent bonds
Most biological polumerizations reactions are?
condensation (dehydration) reactions
3 Properties of a condensation reaction
1) h20 molecule released per polymerization reaction
2)Requires energy
3) Generaly catalyzed by enzymes
The break down of a polymer into monomers occurs during what type of reaction
Hydrolysis reaction
Properties of a hydrolusis reaction
1) 1 H2O Molecule consumed per subunit released
2) Catalyzed by enzymes
Protein
organic macromolecule that consists of 1 or more polypeptide chains folded and coiled into a specific functional conformation
Peptide
short linear polymer of amino acid subunits linked by peptide bonds
Polypeptide
long linear polymer of amino acid subunits linked by peptide bonds
3 classes of amino acids
(based on side chain
1 polar
2 nonpolar
3 charged
Peptide bond formation is a result of
Dehydration reactions between amino acids
the other names for n-terminus and c-teminus
amino terminus and carboxyl terminus
Formula for alpha helices
n-h of amino acid i acts as e donor with carboxyl of i+4
beta sheets
adjacent amino acids alternate between amine and carboxyl groups participating in bonds
primary structure
arrangement of amino acids in linear form
secondary structure
how a single polypeptide twists and pleats due to hydrogen bonds
tertiary structure
the polypeptide forms additional hydrogen bonds, van der waals interactions and disulfide bonds with its side-chain and backbone atoms
quarternary structure
the interactions between the side chain and backbone atoms of more than one polypeptide in a macromolecule
The most common exergonic reaction used in coupling is?
ATP hydrolysis
Coupling is?
Using an exergonic reaction to power a endergonic reaction
1st law of thermodynamics
Energy cannot be created or destroyed
2nd law of thermodynamics
Everytime energy is changed the entropy of the universe

(some energy is lost as heat in biological reactions)
ATP hydrolosis
ATP + H2O --> ADP + Pi
and
delta g=-13kcal/mol (of atp hydrolyzed)
Enzymes speed up reactions by
Reducing the energy of activation or Ea
Transiton state
unstable condition of reactants that have absorbed enough energy for reaction to proceed
Enzymes orchestrate which metabolic reactions occur and when by?
Controlling the concentration of enzymes
Enzyme cycle
enzyme + subsrtates(s) -->
enzyme substrates(s) complex-->
products +enzyme
Active site
site on the enzyme where the reactions is catalyzed (usually the substrate binding site)
Binding site
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
Why can a small amount of enzyme catalyze a large amount of the production of a product
1) Enzyme is unchanged in reaction
2)Weak bonds between enzyme and product can be broken relatively easily
Turnover rate
amount of product produced/an enzyme/second
How do enzymes lower activation energy
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
Enzyme saturation
When all available active sites are engaged
irreversible inhibitor
a substance that selectively (specific enzymes) attaches to an enzyme via covalent bonds and acts as an inhibitor, cannot be sepperated
Reversible inhibitor
Inhibitor which connects to an enzyme via weak ineractions. can be removed.
competitive inhibitor
a substance which resembles substrate and competes for the binding site

*can be overcome by adding more substrate
non-competitive inhibitor
a substance which binds to an area of the enzyme which is not the active site

*cannot be overcome by adding more substrate
cofactor
substance which helps enzyme catalyze a reaction eg. vitamins or Mg2+
Allosteric regulation
regulator molecule binds at allosteric site and shifts equilibrium toward active or inactive conformation
Allosteric activator
molecule that shifts equilibrium toward active conformation
Allosteric inhibitor
molecule that shifts equilibrium toward inactive conformation
feedback inhibition
down-regulation of a metabolic pathway by its end product via the inhibition of an enzyme that catalyzes and early reactions in the pathway
enzyme cooperativity
binding of substrate to one active site increases the binding of additional substrates to additional active sites in the enzyme
nucleic acid
polymer of nucleotide monomers linked via phosphodiester linkages
2 types of nucleic acid
ribonucleic acid RNA
deoxyribonucleic acid DNA
Nucleotide consts of what 3 parts?
-5 carbon sugar
-phosphate group
-nitrogenous base
Which Carbon is the phosphate attached to?
5'
Which carbon is the nitrogenous base attached to?
1'
pyrimidines
6 membered ring
3 kinds:
cytosine-c-both dna rna
thymine-t-dna only
uracil-u-rna only
purines
double ring structure
guanosine-g-both dna rna
adenine-a-both dna rna
Phosphodiester linkage
connects two nucleotides by connecting the 3' carbon of nucleotide "n" with the 5' carbon of nucleotide 'n+1"
Two end of linear polymer
begins at 5' end
ends at 3' end
how does dna sequence determine protein sequence
dna-------->rna--------->protein transcription translation
pyrimidines
6 membered ring
3 kinds:
cytosine-c-both dna rna
thymine-t-dna only
uracil-u-rna only
purines
double ring structure
guanosine-g-both dna rna
adenine-a-both dna rna
Phosphodiester linkage
connects two nucleotides by connecting the 3' carbon of nucleotide "n" with the 5' carbon of nucleotide 'n+1"
Two end of linear polymer
begins at 5' end
ends at 3' end
how does dna sequence determine protein sequence
dna-------->rna--------->protein transcription translation
what is a codon
a set of 3 nitrogenous bases in DNA/RNA

64 possible codons (4^3) for 20 amino acids
Ribosome
enzyme that catalyzes synthesis of polypeptide is