-
the universal solvent
Takes up 70 to 80 percent of a cell's mass
Polar molecules that can hydrogen bond
Water
-
water's ability to ______ allows it stay liquid at room temp.
This ability also provides strong cohesive forces between water molecules.
Hydrogen bonding
-
WATER FEARING MOLECULES
Strong cohesive forces, provided by hydrogen bonding, squeeze this molecule away from water and causes them to aggregate.
hydrophobic molecules
-
Water loving molecules that dissolves easily in water
hydrophilic molecules
-
Most macromolecules of living cells are broken apart with the addition of water. This process is called _________.
Hydrolysis
-
Most macromolecules of living cells are formed with the removal of water
dehydration
-
any biological molecule that has low solubility in water and high solubility in non-polar organic solvents.
a lipid
-
six major groups of lipids
fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes
-
The building blocks for most complex lipids.
They are long chains of carbons truncated at one end by a carboxylic acid.
Usually an even number of carbons with the max being 24 in humans.
Can be saturated or unsaturated.
Fatty acids
-
Fatty acids that possess only single carbon-carbon bonds
Saturated fatty acids
-
Fatty acids that contain one or more carbon-carbon double bonds
Unsaturated fatty acids
-
This lipid is constructed from a three carbon backbone called glycerol.
their function is to store energy. They may also function to provide thermal insulation and padding to an organism
triacylglycerols or triglycerides or fats and oils
-
These fat cells are specialized cells whose cytoplasm contains almost nothing but triglycerides
Adipocytes
-
This lipid is also built from a glycerol backbone but a polar phosphate group replaces one of the fatty acids. This lipid is amphipathic
phosholipids
-
This marcomolecule is built from a chain of amino acids linked together by peptide bonds. They are sometimes referred to as polypeptides.
Proteins
-
The number and sequence of amino acids in a polypeptide is called ______
the primary structure
-
Once the primary structure is formed, the single chain can twist in to an _____________ or lie along side itself and form a __________
alpha helix, beta-pleated sheet
-
Alpha helix and beta pleated sheets are a part of which structure?
Secondary structure
-
This Structure is the 3-dimensional shape that is formed when the peptide chain curls and folds.
Tertiary structure
-
When two of more polypeptide chains bind together, they form this structure.
Quaternary structure
-
When the conformation is disrupted, the protein is said be _______.
Denatured
-
This macromolecule is made off of carbon and water with the empirical formula C(H2O).
aka sugars or saccharides
carbohydrate
-
Five and six carbon carbohydrates are the most common in nature. The six carbon carbohydrate called _____ is the most commonly occurring sugar of all the six carbon sugars.
Glucose
-
Animals eat _______ linkage but only bacteria break down _______ linkage
alpha, beta
-
glucose and starch have _____ linkage so they can be consumed by animals.
alpha
-
Cellulose has _____ linkage, so animals that consume cellulose must have certain type of bacteria in their stomach to digest it.
beta
-
This carbohydrate is made from glucose. They are found in all animal cells and have large amount in muscle and liver cells. have alpha linkages
Glycogen
-
This macromolecule is composed of three components: a five carbon sugar
a nitrogenous base
a phosphate group
nucleotide
-
Nucleotides form polymers to create _____________ such as DNA and RNA
Nucleic acid
-
The type of bonds nucleotides use to form nucleic acids
phosphodiester bonds
-
This nucleotide is the source of readily available energy for the cell
ATP (adenosine triphosphate)
-
This nucleotide is an important component in many second messenger systems.
cyclic AMP
-
These nucleotides are the coenzymes involved in the Krebs cycle
NADH and FADH2
-
The dissolved inorganic ions inside and outside the cell. They assist in the transport of substances entering and exiting the cell.
Minerals
-
These globular protiens function as a catalyst for reactions by lowering the activation energy thus speeding up the reaction
enzymes
-
what is the reactant(s) upon which an enzyme works called?
substrate
-
The position on the enzyme where the substrate binds
active site
-
Enzymes are designed to work only on a specific substrate or group of closely related substrate. This design is called:
an example is the lock and key theory and induce fit model.
enzyme specificity
-
This type of enzyme specificity states that the active site of the enzyme has a specific shape that only fits a specific substrate.
the lock and key theory
-
This type of enzyme specificity states the shape of both the enzyme and the substrate are altered upon binding.
the induced fit model
-
In order to reach their optimal activity, many enzymes require a non-protein component called ____________. They are usually minerals or coenzymes.
Cofactor
-
These organic molecules are vitamins that are considered cofactors
coenzymes
-
What are agents that bind covalently to enzymes and disrupt their function?
irreversible inhibitors
-
This inhibitor competes with the substrate by bining reversibly with noncovalent bonds to the active site. Once bonded, the substrate is blocked from bonding.
competitive inhibitors
-
This inhibitor binds noncovalently to an enzyme at a spot other that the active site and change the conformation of the enzyme. There is no competition between inhibitor and and substrate.
noncompetitive inhibtors
-
The modification of the enzyme configuration resulting from the binding of an activatio or inhibitor at a specific binding site on the enzyme.
Allosteric interactions
-
This phenomenon provides a shut down mechanism for a series of enzymatic reactions when that series has produced a sufficient amount of product.
negative feedback
-
This phenomenon occrs when the product returns to activate te enzyme.
Postive feedback (tends to occur less than negative feedback)
-
The change of the enzyme configuation after the binding of feedback inhibitors
allosteric regulation
-
The suffix for enzymes are:
"-ase"
-
This is all cellular chemical reactions. It includes anabolism (molecular synthesis) and catabolism (molecular degradation)
metabolism
-
respiration in which oxygen is not required
anaerobic respiration
-
the first stage of anaerobic and aerobic respiration. It is the series of reactions that break down a six carbon glucose molecule into 3-carbon molecule of pyruvate. other important products in 2 ATP and 2 NADH
Glycolysis
-
the reaction of glycolysis occur in this fluid portion of living cells
the cytosol
-
This anaerobic respiration includes the process of glycolysis, the reduction of pyruvate to ethanol or lactic acid and the oxidation of NADH to NAD+
Yeast produce ethanol and muscle cells produce lactic acid as waste product as well as CO2
Fermentation
-
RESPIRATION THAT REQUIRES OXYGEN.
aerobic respiration
-
The products of glycolysis will move to this part of the mitochondria if oxygen is available and the cell is capable of aerobic respiration
matrix of a mitodchondrion
-
This membrane is not very permeable. Pyruvate moves through it using facilitated diffusion. Once pyruvate is passed the membrane and is inside the matrix, it is converted into acetyl CoA in a reaction that produces NADH and CO2
Inner Mitochondrial Membrane
-
This is a coenzyme that transfers two carbons from pyruvate to the four carbon oxaloacetic acid to begin the Kreb cycle aka the citric acid cycle.
ACEtyl CoA
-
Each turn of this cycle produces 1 ATP, 3 NADH and 1 FADH2
Kreb Cycle or the Citric Acid Cycle
-
Aerobic respiration produces about this many net ATP
36
|
|