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85 Cards in this Set

  • Front
  • Back
Solvent in which the chemical reactions of living cells take place. Makes up 70-80% of the cell's mass.
Water
Water molecules are held in place by this type of bond.
Hydrogen bond
hydrophobic
"water-fearing"; molecules that are hydrophobic do not dissolve in water.
hydrophilic
"water-loving"; molecules that are hydrophilic dissolve in water.
Water molecules ________ hydrophilic molecules, separating them from the group.
solvate (surround)
Hydrolysis
The most prevalent catabolic reaction in the body.
Dehydration synthesis
An anabolic reaction that removes water in order to synthesize a reaction.
The greater ratio of lipid to protein, the _____ the density.
Lower. Lipoproteins in order from least to most dense: VLDL, LDL, HDL.
Name the four levels of protein structure.
1. amino acid sequence
2. a helix/ beta pleated sheets
3. twisted polypeptide/ 3D folding
4. Several polypeptides bound together.
Which type of bond exists between two cysteine amino acids?
disulfide bond
Denature
Protein loses most of its secondary, tertiary, and quarternary structure.
Minerals
dissolved inorganic ions that assist in the transport of substances entering and exiting the cell.
Enzymes
Typically globular proteins that act as catalysts in the body.
Catalyst
Lowers the energy of activation for a biological reaction and increases the rate of that reaction.
Substrate
The reactant upon which the enzyme works.
Active Site
The position on the enzyme to where the substrate binds.
The enzyme bound to the substrate is specifically called the ____________
Enzyme-substrate complex
Enzyme specificity
The idea that enzymes are designed to work only on a specific substrate or group of closely related substrates.
Lock and key theory
Theory that states that the active site of the enzymes has a specific shape like a lock that only fits a specific substrate, the key. This theory explains some, but not all enzymes.
Induced fit theory
The shape of both the enzyme and the substrate are altered upon bonding.
Saturation kinetics
As the relative concentration of a substrate increases, the rate of the reaction also increases, but to a lesser and lesser degree until a maximum rate (asymptote when graphed) has been achieved.
Cofactor
Coenzymes or metal ions required to assist enzymes.
Coenzymes
Organic molecules that help enzymes reach their optimal activity. They usually exist as vitamins.
Zymogen/proenzyme
The inactive form of an enzyme.
Metabolism
The sum of all the body's cellular chemical reactions.
Anabolism
molecular synthesis
Catabolism
molecular degradation
Respiration
The "energy aquiring" stage of metabolism where oxygen can be used or not used.
Anaerobic respiration
respiration in which oxygen is not required
Glycolysis
first stage of aerobic and anaerobic respiration; breaks 6-carbon molecules of glucose into 3-carbon pyruvate. The process of glycolysis alone produces 2 ATP.
Pyruvate
A broken down form of glucose that aids in respiration.
Cytosol
Fluid portion of living cells; glycolysis takes place here.
Substrate level phosphorylation
The formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion.
Aerobic respiration
requires oxygen
If the cell has oxygen available, the products of glycolysis will move into the ____________ to continue the process of aerobic respiration.
mitochondrion matrix
Inner mitochondrial membrane
Less permeable membrane that allows pyruvate to move through but not all NADH molecules.
acetyl CoA
Converted from pyruvate and acts as the junction between glycolysis and the citirc acid cycle.
Krebs Cycle
Immediately following glycolysis, each turn of the Krebs cycle creates 1 ATP, 3 NADH, and 1 FADH2. CO2 is given off as a waste product.
The final electron receptor at the end of the electron transport chain is __________
oxygen
In a human renal cortical cell, the Krebs cycle occurs in the ______________
mitochondrion matrix
As electrons move within the electron transport chain, each intermediate carrier molecule is
reduced by the preceding molecule and oxidized by the following molecule.
Which process do aerobic and anaerobic respiration share?
Glycolysis
Name the products of glycolysis.
ATP and pyruvate
What is the net ATP production from fermentation?
2 ATP
Do lipids contain polymers?
no
Examples of lipids
fats, phospholipids, steroids
why are fats hydrophobic?
Because of the relatively nonpolar C-H bonds in the hydrocarbon chains of fatty acids
Is the head hydrophobic or hydrophilic?
phobic
What are lipids composed of?
glycerol+3 fatty acids
Difference between saturated vs. unsaturated fatty acids
saturated have single bonds, unsaturated have double
Triaglycerols have a 3 carbon backbone called _________
glycerol
fats and oils are more formally called _______________
Triaglycerols
What type of lipid is especially suited for the major component of membranes?
phospholipids
Four ringed structures are _______
steroids
what does 'amphipathic' mean?
one end is polar, the other isn't
give an example of an amphipathic lipid
phospholipid: a polar phosphate end, and nonpolar fatty acid end
Proteings are built from _____ _______
amino acids
what are amino acids linked by?
peptide bonds
how many alpha amino acids are there?
20
How many amino acids are "essential"? what does "essential" mean?
10, must be ingested directly
R group is also known as a
____ ______
side chain
structural proteins are made from _____ _________
long polymers
collagen is what type of protein?
structural
what is the chemical formula of a carbohydrate?
C(H2O)
Gie the three componenets of a nucleotide:
1. A five carbon sugar (pentose)
2. a nitrogenous base
3. a phosphate group
Give the most common nitrogen bases:
adenine, guanine, cytosine, thymine (DNA), and uracil (RNA)
what type of bonds are found in DNA?
phosphodiester bonds
Adenine and thymine form ___ hydrogen bonds, while cytosine and guanine form ___
2, 3
What is an example of a catabolic rxn?
hydrolysis, breaks from complex to simpler
which is digestible by animals, starch or cellulose?
starch
Give examples of metal ion cofactors:
Fe, Cu, Mn, Mg, Ca, Zn
Agents which bind covalently to enzymes and disrupt their function are _______ inhibitors
irreversible
Bind reversibly with noncovalent bonds= _______ inhibitors
competative
Bind noncovalently and change the conformation of the enzyme= ______ inhibitors
noncompetative
Negative feedback acts in what direction of the stimulus?
against, shuts its shit down
Positive feedback acts in what direction of the stimulus?
with it
All of the following must chanfe the rate of an enzyme-catalyzed rxn except:
-changing pH
-lowering temp
-decreasing the concentration of substrate
-addaing a noncompetative inhibitor
decreasing concentration of substrate
Why wouldn't one use heat to accelerate a rxn?
heat changes the configuration of proteins
Fermentation is what type of respiration?
anaerobic
STUDY KREBS CYCLE
STUDY KREBS CYCLE
What is the electron transport chain (ETC)?
The ETC is a series of proteins, including cytochromes with heme
the final electron receptor in the ETC is...
O2
where does the Krebs cycle occur?
the mitochondrial matrix
Say whether each is aerobic or anaerobic:
fermentation
Krebs
glycolysis
oxidative phosphorylation
anarobic
aerobic
both
aerrobic
What is the net ATP production from fermentation?
2 ATP