TEST REVIEW- UNIT 1- chapter 5 & 8 Flashcards
What is a monomer?
Single/individual unit
What is a polymer?
Long chain of repeating (monomers) units
What do enzymes end with?
-ase
What are the polymers of carbohydrates?
Starch, glycogen, Cellulose, amylose, chitin
What are polymers of lipids?
Lipids dont have polymers
What is the protein monomer?
Amino acids
What is different about amino acids?
They have different R groups
Monomer of lipids
Glycerol, fatty acid, steroids
Functions of protein are:
Structure
Function
Defense
Hormonal
Transport
Coordination
What bonds hold proteins together?
A peptide bond
What is the polymer of proteins
polypeptide
What is the polymer of nucleic acids?
Polynucleotide
/What are the steps of tertiary structure of protein conformation?
Primary
Secondary
Tertiary
Quatenary
What is primary structure of protein conformation?
Are the linear sequence of amino acids
Structure is determined by amino acid sequence
— constructed by peptide bonds
What stage of protein confirmation cannot be further broken down?
— the stage where nothing can be further broken down is the primary structure. Cannot break down he covalent bonds
Explain secondary structure/step of protein confirmation
Results from hydrogen bonding along polypeptide backbone
—this hydrogen bonding results in alpha (HELIX) and beta (PLEATED) sheets.
Sickle cell anemia results from a mutation that replaces glutamic acid residue with which of the following?
Arraigning
Asparagine
Lysine
Glutamine
Aspartic Acid
Lysine
Explanation- single amino acid substitution from glutamic acid to lysine is responsible for sickle cell anemia.
What is sickle cell anemia?
Mutation that occurs in gene that codes for hemoglobin and causes misfolding that results into lower oxygen affinity. Crescent shape
The __________ structure of protein corresponds to linear order of amino acids in given polypeptide chain.
Primary
When protein is transferred to a solution with a pH lower than its optimal range, which of the levels of protein structure is/can be affected?
Secondary, tertiary, quaternary.
What is the most important stage of protein confirmation?
Primary
The formation of peptide bond is example of what type of reaction?
DEHYDRATION SYNTHESIS
Condensation reaction
— when two amino acids come together, a water molecule is let go
Which level of protein structure is affected by sickle cell anemia?
Primary
Explains the tertiary structure of protein confirmation…
Stage where the
OVERALL 3-D STRUCTURE OF POLYPEPTIDE IS FORMED. This is due to interactions between R groups of amino acids that make up proteins
Explain the quaternary stage of protein confirmation…
The association of several protein/polypeptide subunits are closely packed to form a larger structure.
Forms function of protein
SUBUNITS ARE HELD TOGETHER BY HYDROGEN BONDS AND VAN DER WALLS BETWEEN NON-POLAR SIDE CHAINS
Example of proteins with quaternary structure:
Hemoglobin, DNA< polymerase, ribosomes, antibodies
All enzymes end in -ase. What is the exception?
Trypsin and pepsin enzymes have protein ending -in
What factors affect enzyme activity?
Temperature, pH, salinity (salt concentration), concentration (of substrate or enzyme)
What happens to enzyme activity if there is more enzyme concentration?
Increase enzyme concentration===== speeds up reaction only until saturation
What is (point of) saturation?
When all active sites of an enzyme are occupied.
THE POINT WHEN MORE SUBSTRATE WILL NOT INCREASE RATE OF REACTION
There are concentration of substrates and enzymes, the substrates try to find active sites to fit into. Once all active sites are filled up, that is point os saturation.
What is activation energy?
Energy needed to get a reaction started
What role do catalysts have in rate of reaction?
Most enzymes catalyze in one direction
CATALYSTS SPEED UP REACTIONS BY LOWERING AMOUNT OF ACTIVATION ENERGY
What is a substrate?
Substance on which enzymes react
How many substrates can an enzyme fit?
1 substrate per enzyme
What is the active site of an enzyme?
Part of enzyme to which substrate bind and where reaction is catalyzed
What is induced fit?
When enzyme and substrate collides- the enzyme squeezes to get as close to the substrate as possible.
—WHEN THEY GET CLOSE, atoms alter bonds
What does induced fit have to do with activation energy?
When enzyme and substrate are healed close together and squeeze, it takes less energy to overcome a bond and break it.
