Study your flashcards anywhere!

Download the official Cram app for free >

  • Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key

image

Play button

image

Play button

image

Progress

1/54

Click to flip

54 Cards in this Set

  • Front
  • Back
hydrogen bond
bond that allows water to maintain its liquid state by providing strong cohesive forces between molecules
hydrophobic
cohesive forces of water squeeze hydrophic molecules away
hyrophilic
dissolve easily in water because they are 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:
-fatty acids
-traicylglycerols
-phospholipids
-glycolipids
-steroids
-terpenes
fatty acids
building blocks of lipids, long chains of carbons with carboxylic acid end
Triacylglycerols/triglycerides
-lipids
-fats and oils with a three carbon backbone called glycerol
adipocytes
specialized fat cells whose cytoplasm contains mostly triglycerides
phospholipids
-built of glyerols but have a polar phosphate group, polar at the phosphate end, nonpolar at the fatty acid end (amphiphatic)

-think membranes!
Proteins/polypeptides
-built from amino acids linked together by peptide bonds

-all proteins from 20 acids, 10 essential (not in body)

-only differ from one another by r group or side chains
amino acid structure
R
H2N-CH-COOH
primary structure
number and sequence of amino acids
secondary structure
formation of alpha-helix or Beta pleated sheets(parallel or antiparallel)

-reinforced by hydrogen bonding(disrupted by proline)

-conformation of protein
tertiary structure
three dimension shape created 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 conformation is disrupted
Collagen
most abundant protein in the body
glycoproteins
proteins with carbohydrate groups attached
cytochromes
proteins that add color to the cell
Carbohydrates
made from carbon and water, most common: glucose
glucose
-most common carbohydrate

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

-is oxidized for ATP or is polymerized to glycogen

-liver regulates blood glucose level

-end product of carbohydrate digestion
Starch and cellulose
-found in plants only

-formed from glucose
alpha linkages/ beta linkages
animals digest alpha linkages like that of starch and glycogen but bacteria can only 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 to Thymine (2H bonds)

-Guanine to cytosine (3H Bonds)

-top 5-3, bottom 3-5
RNA
-single stranded

-Uracil replaces Thymine
Minerals
dissolved inorganic ions
Enzymes
globular proteins that act as a catalyst
catalyst
-lowers the energy of activation for a reaction

-increases the rate of reaction

-not consumed found in reactants and products

-only small amount required

-does not alter equilibrium concentrations
substrates
reaction or reactants an enzyme works on
active site
position on enzyme where substrate bonds
enzyme substrate complex
name for when enzyme is bound to substrate
enzyme specificity
enzymes can only work on a specific substrate or group of closely related substrates: example- lock and key theory
induced fit theory
shape of enzyme and substrate are both altered upon binding
saturation kinetics
-as level of substrate increases so does rate of reaction, but increases lesser and lesser until it Vmax is reached

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

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

-can be coenzymes or metal ions or minerals

-many are vitamins or derivates of vitamins
Enzyme inhibition
-process of inhibiting enzymes

-irreversible inhibitors: cant be reversed
competitive inhibitors
-compete with substrate for active site

-resemble substrate

-increased substrate concentration overcomes competitve inhibitors

-increases Km but does not alter Vmax
noncompetitive inhibitors
-bind noncovalently to an enzyme at a spot other than the active site and change the conformation of the enzyme

-cannot be overcome

- lowers Vmax, Km unchanged (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 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
shuts down mechanism when it has produced sufficient product
positive feedback
product returns to activate the enzyme
positive/negative cooperativity
change in shape of enzyme from allosteric regulation can allow other substrates to bind more easily(positive) or not so easily (negative)
enzyme classification
-end in ase

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

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

kinase: phosphorylates to activate or deactive
phosphatase
Glycolysis
-occurs in both anaerobic and aerobic respiration

-breaks 6-carbon glucose into 2 3 carbon molecules

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

-nets 2 ATP and 2 NADH

-associate with pyruvate and NADH

-occurs in cytosol (all living cells can do this)

-3rd step is irreversible where the second phosphorylation 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 2 ATP
Fermentation
-anaerobic process

-recycles NADH back to NAD+

-includes glycolysis and produces 2 ATP
Enzymes and Cellular Metabolism
When enzymes are inhibited by poision, there will be a build of of reactants and a dramatic reduction in products of the reaction which enzymes govern.
Aerobic respiration
-requires oxygen

-works on products of glycolysis(pyruvate and NADH)

-occurs in the MATRIX of the mitochondria

-inside matrix pyruvate-> acetyl CoA

-produces 36 net ATPs, 1 NADH -> 2-3 ATPs, 1 FADH2 -> 2 ATPs
Kreb Cycle
-each turn prodcutes 1 ATP (through substrate-level phosphorylation)

-3 NADH and 1 FADH2

-part of aerobic respiration, occurs in mitochondria matrix

-1 glucose = 2 turns
Respiration
Glucose + 02 -> CO2 + H20
Electron Transport Chain
-a series of proteins including cythochromes in the inner membrane of the mitochondria

-oxidizes NADH and ultimately accepted by OXYGEN

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

-each intermediate molecule is reduced than oxidized