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125 terms

BIO 1: Molecular Bio and Cell Resp (MCAT)

MCAT
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The 6 lipids
fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes
triacylglycerol
They store metabolic energy and provide thermal insulation and padding.
glycerol
A simple polyol compound. It is a colorless, odorless, viscous liquid that is widely used in pharmaceutical formulations. It has three hydroxyl groups that are responsible for its solubility in water and its hygroscopic nature.
polyol
An alcohol containing multiple hydroxyl groups.
phospholipid
Structural components of membranes.
glycolipids
Are lipids with a carbohydrate attached.
steroids
They regulate metabolic activity.
terpenes
A large and diverse class of organic compounds, produced by a variety of plants, particularly conifers.
fatty acids
Some serve as local hormones, such as eicosanoids.
hydrogen bond
The attractive interaction of a hydrogen atom with an electronegative atom, such as nitrogen, oxygen or fluorine, that comes from another molecule or chemical group.
hydrolysis
The process of splitting a compound into fragments with the addition of water; a kind of reaction that is used to break down polymers into simpler units, e.g. starch into glucose.
amphipathic
Of, or relating to, a molecule having hydrophobic and hydrophilic regions.
Van der Waals forces
The attraction or repulsion of forces because of already created or quickly induced dipoles.
protein
A molecule composed of polymers of amino acids joined together by peptide bonds. It can be distinguished from fats and carbohydrates by containing nitrogen.
amino acid
The building block of protein in which each is coded for by a codon and linked together through peptide bonds. Has NH2 and COOH in it.
peptide bond
The covalent bond joining amino acids, particularly at the carboxyl group of one amino acid to the amino group of the other amino acid, with the concomitant release of a molecule of water.
polypeptide
Other name for proteins.
10
How many amino acids are essential to humans?
essential
_____ amino acids are ones that must be ingested because the body can't make them.
side chains
Amino acids differ in this structurally. They are also called R groups.
primary structure
Sequence of amino acids in a polypeptide.
secondary structure
Deal with the conformation of a protein and may be an α-helix or a β-pleated sheet.
tertiary structure
The 3D structure that may arise from large proteins when they clump together onto themselves.
quarternary structure
When two or more polypeptide chains bind together.
denatured
When the conformation of a protein is disrupted. If the agent that does this is removed, it can go back to normal.
globular, structural
Two types of proteins?
collagen
Most abundant protein in the body and is a a structural protein.
proteoglycan
Mixture of proteins and carbohydrates that is mostly carbohydrates.
cytochrome
A class of hemoprotein found in mitochondria that transport electron or protons.
conjugated
Proteins with nonproteinaceous components are called _______ proteins.
glucose
The most commonly occuring six-carbon carbohydrate.
anomer
Stereoisomers of a sugar which differ only in how they are configured about their respective carbonyl (anomeric) carbon atom.
animals
In glucose, ____ break alpha linkages.
bacteria
In glucose, ____ break beta linkages.
glucose
Plants make starch and cellulose from what?
amylose, amylopectin
Starch comes in these two forms.
isomer
Amylose is an ____ of cellulose.
isomer
One of two or more molecules that have the same chemical formula but have a different stereochemical arrangement of their atoms.
animals, bacteria
____ digest glycogen, ____ digest cellulose.
nucleotide
Made of a five-carbon sugar; a nitrogenous base; and a phosphate group.
nitrogenous bases
Adenine, guanosine, cytosine, thymine, and uracil.
phospholipid bonds
The bonds that hold nucleic acids together to make DNA and RNA.
third
Phospholipid bond is made from the phosphate group of one nucleotide and the __ carbon of the pentose on the other nucleotide.
adenine
What binds with thymine?
thymine
What binds with adenine?
cytosine
What binds with guanine?
guanine
What binds with cytosine?
top
The (top/bottom) strands runs 5'->3'.
bottom
The (top/bottom) strands runs 3'->5'.
uracil
What replaces thymine in RNA?
nucleotide
ATP is a (protein/carbohydrate/nucleotide/lipid).
cyclic AMP
Abbreviation for cyclic adenosine monophosphate, a second messenger essential in many biological processes of various organisms.
minerals
The dissolved inorganic ions inside and outside the cell. They can also assist as cofactors.
cofactor
An inorganic complement of an enzyme reaction, usually a metal ion.
enzyme
Globular proteins that act as a catalyst, lowering the energy of activation for reactions to increase the rate of reaction.
no
Are enzymes consumed in a reaction?
no
Do enzymes alter equilibrium of a reaction?
substrate
Reactant which enzyme uses.
active site
Place where substrate bonds to enzyme.
enzyme specificity
When an enzyme is made for a certain substrate that fits in a certain way.
induced fit
When the enzyme and substrate alter their shape a little to fit together.
saturation kinetics
As more substrate is added, the rate of a reaction increases, but it starts to level off at some point.
yes
Does temperature affect reaction rate?
yes
Does pH affect reaction rate?
37
What is the degrees Celcius for the best temperature for enzymatic reactions.
metal ions
Cofactors can be coenzymes or ______.
vitamins
Many coenzymes are _____ or their derivatives.
competitive, irreversible, noncompetitive
The three types of enzymatic inhibition are?
competitive inhibition
Something blocks the substrate at the active site from binding to the enzyme. This is reversible.
noncompetitive inhibition
It changes the conformation of the enzyme so that the substrate can't bind to the enzyme's active site.
irreversible inhibition
When something blocks the enzyme's ability to function by binding to it. Not reversible.
enzymes
Proteolytic cleavage, reversible covalent modification, control proteins, and allosteric interactions. What do these four regulate?
zymogen
Inactive form of an enzyme.
proenzyme
Inactive form of an enzyme.
cleavage of peptides
A zymogen/proenzyme is activated by ___ _ ___.
-ogen
Suffix for a proenzyme/zymogen?
yes
Are some enzymes activated or deactivated by phosphorylation?
control proteins
These are protein subunits that activate or inhibit enzymes, like G-proteins.
allosteric regulation
The modification of an enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme.
negative feedback
When the creation of end product stops the reaction from going on.
positive feedback
When the creation of end products makes it make more product.
positive cooperativity
When a substrate binds to an enzyme, making it easier to bind with more substrate.
negative cooperativity
When a substrate binds to an enzyme, making more substrate harder to bind to the enzyme.
-ase
Suffix for an enzyme?
kinase
A (kinase/phosphatase) is an enzyme that phosphorylates something.
phosphotase
A (kinase/phosphatase) is an enzyme that dephosphorylates something.
ligand
An ion or molecule that binds to a central metal atom to form a coordination complex.
metabolism
All cellular chemical reactions.
anabolism
Molecular synthesis.
catabolism
Molecular degradation.
three parts of metabolism
1) Macromolecule catabolism, 2) Oxidized to acetyl CoA, pyruvate, other metabolites, 3) If oxygen available, mixes with metabolites to citric acid cycleto make energy.
respiration
Energy-aquiring stage in the metabolism.
aerobic, anaerobic
2 types of respiration?
anaerobic resipration
Respiration where oxygen is not needed.
glycolisys
First stage of anaerobic and aerobic respiration. Breaks 6-carbon glucose molecule to 2 3-carbon molecules of pyruvate.
pyruvic acid
Pyruvate conjugate?
yes
Does glycolysis act where there is and isn't oxygen?
cytosol
Where does glycolysis occur?
no
Can phosphorylated molecules go through the membrane?
substrate level phosphorylation
The 3-carbon molecules in respiration give up one phosphate to make ADP into ATP.
mono
Fructose and glucose are ___-saccharides.
2, 4
In respiration, _ ATP are spent and _ ATP are made.
glucose
Galactose can be converted to ____ to then be used in respiration.
fermentation
A name for anaerobic respiration.
lactic
Fermentation has glycolysis and the ____ acid cycle.
NADH, pyruvate
Fermentation occurs with the lack of oxygen or when there isn't enough ____ and ____.
NAD+
Fermentation turns NADH into ____.
aerobic respiration
Respiration that requires oxygen.
matrix of a mitochondrion
If anaerobic respiration is possible, glycolysis product goes to ___.
inner
Which part of the mitochondrion is less permeable? Inner or outer?
acetyl CoA
When pyruvate is inside the matrix of the mitochondrion, it is turned into ____, and CO2 is released.
coenzyme
Is acetyl CoA an enzyme or coenzyme?
1 ATP, 1 FADH2, 3NADH
Krebs cycle makes ___, ____, and ___, and is called substrate-level phosphorylation.
electron transport chain
This couples electron transfer between an electron donor (such as NADH) and an electron acceptor (such as O2) with the transfer of H+ ions (protons) across a membrane. The resulting electrochemical proton gradient is used to generate chemical energy in the form of adenosine triphosphate (ATP).
mitochondria
Where is the electron transport chain?
oxygen
Electrons go down the ETC to be accepted by ____.
protons
As electrons are passed down the ETC, ____ are pumped into the membrane.
proton-motive force
The energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work.
ATP synthase
An enzyme that catalyzes the formation of ATP from the phosphorylation of ADP with inorganic phosphate, using a form of energy, such as the energy from a proton gradient.
2
Net ATP production from fermentation?
oxidative phosphorylation
A metabolic pathway that generates ATP from ADP through phosphorylation that derives the energy from the oxidation of nutrients.
products
____ of respiration: oxygen + CO2 + H2O
reactant
____ of respiration: glucose
combustion
What kind of reaction is respiration?
36
How many ATP made in aerobic respiration?