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Difference between dehydration synthesis and hydrolysis
Dehydration synthesis bonds monomers together while hydrolysis separates monomers
What bonds are formed in a primary structure
Peptide bonds
What are peptide bonds
Strong covalent bonds
The structure of an enzyme is determined by what
Its amino acid sequence
What bonds are formed in a secondary structure
Hydrogen bonds
What bonds are formed in a tertiary and quaternary structure
Hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions
Difference between tertiary and quantinary structure
Tertiary is one peptide chain while quantinary involves multiple peptide chains linked together
What structure is a protein when it is denatured
Primary structure
How does a protein change structures
Through reactions to other substances and through chemical interactions
What do R groups do in tertiary and quaternary structure
R groups determine the overall folding, shape, and function of the protein
What does the amino acid sequence have to do with R groups and the function of the protein
The amino acid sequence has R groups that determine the shape of a protein which determines its function
What determines if an amino acid is polar/no polar and hydrophilic/hydrophobic
The amino acid’s R group
Are Enzyme and substrates reactants?
Enzymes are a catalyst while a substrate is a reactant
What is activation energy/Ea Barrier
It is the minimum amount of energy needed to cause a reaction
What do Enzymes do to the Ea barrier and how?
It lowers it because an enzyme increases reactions by requiring less energy for a reaction to occur
Does Exergonic absorb or release energy
It releases energy
Does endergonic absorb or release energy
It absorbs energy
Products is lower than reactants
Exergonic
Products are higher than reactants
Endergonic
True or false: exergonic is spontaneous
True
True or false: endergonic is not spontaneous
True
In between which phosphate groups have the most energy
The second and third phosphate group
What does it mean to be spontaneous in biology
Something that occurs without energy needing to be put into it
What forms when the phosphate bond is broken
ADP forms (has less energy)
What is an enzyme
A biological catalyst (speeds up chemical reactions)
How does an enzyme speed up a reaction
By reducing the activation energy less energy is needed to create a reaction (compared to substances without enzymes which need more energy to create a reaction)
What is the active site
The area of an enzyme which connects to a substate to create a reaction
What is enzyme specificity
Enzymes being able to pick and pair with a substrate with a similar shape (corresponding shape)
What happens when enzymes gets cold (discuss reaction rate)
Enzymes slow down, slowing their pairing with substrates and decreasing the reaction rate
What happens when enzymes get hot (discuss reaction rate)
The enzymes speed up, speeding up their pairings with substrates, but when too fast it denatures to its primary structure (initial amino acid sequence)
What is pH
How acidic or how basic something is (acid being the least, basic being the most pH)
What molecule is an acid represented by
H+ ions (postive hydrogen ions)
What molecule is a base represented by
OH- ions hydroxide ions)
What term means a high pH level
Basic
What term means a low pH
Acidic
What can too much salinity do to an enzyme
It can break the bonds of the enzyme and denature it, changing its shape
Concerning the concentration of a substrate, why does the reaction rate eventually level off
Because there are only so many enzymes that a substrate can be paired with, so the reaction rate will go up as more pair until you run out of enzymes making the reaction rate the same
Concerning the concentration of an enzyme, why does the reaction rate eventually level off
Due to the fact that there are only a set about of substrates, so when all are paired up with an enzyme, no more pairings can happen=no reactions can occur=reaction rate stays the same (doesn’t increase nor decrease)
What does enzyme saturation mean
All substrates have been paired with
What is the difference between a cofactor and a coenzyme
A cofactor is a nonorganic molecule while a coenzyme is an organic molecule.
What do cofactors/coenzymes do and how
They speed up the rate of reaction by placing themselves in the active site, allowing a substrate that wouldn’t originally fit to pair with the enzyme (and therefore create a reaction)
What do inhibitors do
They decrease the rate of enzyme reaction
Why would inhibitors need to be used
To kill off unwanted bacteria and diseases
What is a competitive inhibitor
An inhibitor that goes in front of a substrate on the active site to block the substrate from pairing and forming a reaction
What is a noncompetitive inhibitor
An inhibitor that attaches to the allosteric site of an enzyme to change its active site shape so a substrate wouldn’t be able to fit
What is an allosteric site
A site on an enzyme anywhere other than the active site
Which kind of inhibitor is more effective and why
The noncompetitive inhibitor is more effective because even when the substrate concentration is increase, it still works to prevent the enzyme-substrate connection (unlike a competitive inhibitor that wouldn’t work when the substrate concentration is increased)
How does upping the substrate concentration make a competitive inhibitor less effective
With more substrates, there is a higher change that it will go in front of the one inhibitor and pair with the active site before the inhibitor can block it
In denaturation which protein level is unaffected
The primary structure
What can cause the denaturing of an enzyme
Too much heat, salt, or pH
How does denaturing affect the structure of enzymes
It breaks complex bonds and only leaves peptide bonds to function
How does denaturing affect the function of enzymes
It prevents an enzyme from pairing with a substrate, preventing it from doing its job of increasing chemical reactions
What bonds are being broken when denaturation occurs
hydrogen bonds, hydrophobic interactions, ionic bonds, and disulfide bridges
Why does the name amino acid chemically make sense
Because it has an amine/amino group and a carboxyl (acid) group
What’s the acronym to know if something is polar
(O)h (N)o it(S) (P)olar
What is a polypeptide chain
A link of repeating amino acids
True or false: an enzymes specific shape does not determine its function
False
In tertiary structure which bonds are polar and which are nonpolar
All are polar but hydrophobic interactions
Does polar or nonpolar R groups create hydrophobic interactions
Nonpolar (no charges=not attracted to substances with charges like water)
What is quaternary structure held by
R groups
How do you switch a substrate’s name to an enzyme/catalyst
by switching out the last few letters for “ase”
What is hydrogen peroxide’s enzyme specificity
Catalase
What does induced fit/enzyme-substrate complex mean
When a substrate bonds with an enzyme
When writing a chemical equation involving reactants and substances how are they formed
enzyme
Substrate——>Products
Functions of enzymes (only need 2)
-structure
-defense
-transportation
-movement
-communication
-storage
-regulation of chemical reactions
-enzymes
True or false: every enzyme is a protien
True
How many different kinds of amino acids are used to make human protiens
20
Why do H+ ions denature an enzyme?
Because Enzymes denature when it is presented with too much acidity (low pH)
What does the R group need to be to perform hydrogen bonds in a tertiary structure
A functional group
What does the R group need to be to perform hydrophobic interactions in a tertiary structure
Needs to be nonpolar
What does the R group need to be to perform ionic bonds in a tertiary structure
Needs to be a fully charged functional group
What does the R group need to be to perform disulfide bridges in a tertiary structure
Needs to be SH (sulfhydryl)
Name all the fully charged functional groups
-carboxyl
-amino
-phosphate
Note 
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