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54 Cards in this Set

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  • Back
hydrogen bond
bond that allows water to maintain its liquid state by providing strong cohesive forces between molecules
hydrophobic
-cannot dissolve in water

-cohesive forces of water squeeze hydrophobic molecules away
hydrophilic
-description of a molecule that can dissolve easily in water because it is polar
hydrolysis
process by which most living macromolecules are broken apart
dehydration
process by which most macromolecules are formed
lipid
molecule that has low solubility in water and high solubility in nonpolar organic solvents (hydrophobic)

six groups of lipids:
-fatty acids
-triaglycerols
-phospholipids
-steroids
-terpenes
fatty acids
-building blocks of lipids

-long chains of carbons with carboxylic acid end
triaglycerols/triglycerides
-lipids

-fats and oils with a three carbon backbone called glycerol
adipocytes
specialized fat cells whose cytoplasm contains mostly triglycerides
phospholipids
-made of glycerols but have a polar phosphate group, polar at the phosphate end and nonpolar at the fatty acid end (amphiphatic)

-used to make membranes
proteins/polypeptides
-built from amino acids linked together by peptide bonds

-all proteins built from 20 amino acids, 10 of which are essential (not produced in body)

-amino acids only differ from one another by r group or side chains
primary structure
number and sequence of amino acids
secondary structure
-formation of alpha-helix or beta pleated sheets (parallel or anti-parallel)

-reinforced by hydrogen bonding (which can be disrupted by proline)

-confirmation of a protein
tertiary structure
-three dimensional shape

shape formed by:
-covalent disulfide bonds between two cystein amino acids
-hydrogen bonds
-van der waals forces
-electrostatic interactions
-hydrophobic side chains
quaternary structure
two or more polypeptide chains bonded together
denatured
when confirmation is disrupted
collagen
most abundant protein in the body
amino acid structure
R
NH2-CH-COOH
glycoproteins
proteins with carbohydrate groups attached
cytochromes
proteins that add color to the cell
carbohydrates
-made from carbon and water

-most common carbohydrate: glucose
glucose
-most common carbohydrate

-exists in ring and chain form, ring form has two anomers

-is oxidized for ATP or is polymerized to glycogen

-liver regulates blood glucose level

- primary end product of carbohydrate digestion
starch and cellulose
-made from glucose

-found in plants only
alpha linkages/beta linkages
animals digest alpha linkages like that in starch and glycogen but only bacteria can digest beta linkages like that in cellulose
nucleotides
composed of:
-five carbon sugar (pentose)
-nitrogenous base
-phosphate group

-polymers of nucleotides

-form nucleic acids DNA and RNA

-joined by phosphodiester bonds
DNA
-two nucleotide strands joined by hydrogen bonds to make a double helix

-Adenine joins Thymine (2H bonds)

-Guanine joins Cytosine (3H Bonds)

-top 5 -> 3
-bottom 3-> 5
RNA
-singl stranded

-Uracil replaces Thymine
minerals
dissolved inorganic ions
enzymes
globular proteins that act as a catalyst
catalyst
-lowers the energy of activation for a reactoin

-increases the rate of the reaction

-not consumed; found in reactants and products

-only small amount required

-does not alter equillibrium concentrations
substrates
reaction or reactants that an enzyme works on
active site
position on enzyme where subtrate bonds
enzyme substrate complex
name for when an enzyme is bound to a substrate
enzyme specificity
enzymes can only work on a specific substrate or group of closely related substrates

example: lock and key theory
where only one enzyme can only fit into one specific receptor on substrate
induced fit theory
shape of enzyme and substrate are both altered upon binding
saturation kinetics
-as level of substrate increases so does the rate of the reaction, but increases lesser and lesser until Vmax is reached

-Vmax is proportional to the enzyme concentration
factors that affect enzymes
-temperature: as it goes up, reaction rate goes up until the enzyme denatures and the reaction slows

-pH: optimal pH varies for each enzyme
cofactor
-non-protein that allows enzymes to reach optimal activity

-can be coenzymes, metal ions or minerals

-many cofactors are vitamins or are derivatives of vitamins
enzyme inhibition
-process of inhibiting enzymes

-irreversible inhibitors: can't be reversed
competitive inhibitors
-competes with substrate for active site

-resembles substrate

-increased substrate concentration overcomes competitive inhibitors
noncompetitive inhibitors
-bind noncovalently to an enzyme at a spot other than the active site and changes the conformation of the enzyme

-cannot be overcome

-lowers Vmax, Km unchanges (because enzyme affinity for substrate is unchanged)
enzyme regulation
cells must regulate enzyme activity:

-proteolytic cleavage: enzyme is released in inactive form called zymogen or proenzyme
-> bonds are cleaved and enzyme is activated

-Allosteric interactions:

modification of enzyme configuration resulting from binding of an activator (allosteric activators) or inhibitor (allosteric inhibitors) to specific binding site

-allosteric enzymes have several binding sites
negative feedback inhibition
shut down mechanism triggered by the production of sufficient product
positive feedback
product returns to activate the enzyme
positive/negative cooperativity
change in shape of an enzyme from allosteric regulation can allow other substrates to bind more easily (positive) or less easily (negative)
enzyme classification
-end in ase

-lyases: catalyses addition of one substrate to a double bond of a second substrate called a synthase

-ligases: also govern addition reaction but require ATP or other nucleotide

-kinase: phosphorylates to activate or deactivate phosphatase
glycolysis
-occurs in both anaerobic and aerobic respiration

-breaks 6-carbon glucose into two 3-carbon molecules

-has a 6 carbon stage (which uses 2 ATP) and a 3 carbon stage

-nets 2 ATP and 2 NADH

-associate glycolysis with pyruvate and NADH

-occurs in the cytosol (all living things can do this)

-3rd step is irreversible where the second phosphorlation commits the molecule to the glycolytic pathway
substrate level phosphorylation
-formation of ATP from ADP and inorganic phosphate

-occurs at the end of glycolysis to form 2ATP
fermentation
-an anaerobic proess

-recycles NADH back to NAD+

-includes glycolysis and produces 2 ATP
enzymes and cellular metabolism
When enzymes are inhibited by a poison, there will be a build up of reactants and a dramatic reduction in products of the reaction which the enzyme governs.
aerobic respiration
-requires oxygen

-works on products of glycolysis (pyruvate and NADH)

-occurs in the Matrix of the mitochondria

-inside matrix pyruvate -> Acetyl CoA

-net production of 36 ATPs

1 NADH produces 2-3 ATPs
1 FADH2 produces 2 ATPs
Kreb cycle
-each turn produces 1 ATP (through substrate level phosphorylation)

-3 NADH and 1 FADH2

-part of aerobic respiration, occurs in the mitochondria matrix

-1 glucose produces 2 turns of the Kreb cycle
respiration
Glucose + Oxygen -> Water + Carbon dioxide
electron transport chain
-a series of proteins including cytochromes in the inner membrane of the mitochondria

-oxidizes NADH and ultimately accepted by Oxygen

-establishes a proton gradient in the intermembrane space (lower pH than the matrix) which propels protons through ATP synthase to make ATP through oxidative phosphorylation (2-3 ATP per NADH)

-each intermediate molecule is reduced then oxidized