Water is less dense as a solid than as a liquid, due to H bonding. Crystalline lattice keeps molecules at a distance.
Back
Monosaccharides
Front
CH2O=empirical formula
Examples:
glucose- blood sugar
fructose- fruit sugar
galactose
ribose- structural component in RNA
Importance:
-produced by photosynthesis
-used in cellular respiration (to make energy)
-summary: energy storage and release
-also used to build structures
Back
Molecule
Front
elements covalently bonded
Back
What are some substances that are transported in blood?
Front
-NaCl: dissolved in plasma (ions)
-amino acids: dissolved in plasma (sufficient solubility due to charged regions)
-glucose: dissolved in plasma (polar)
-oxygen gas: carried by hemoglobin (nonpolar)
-fats: transported in lipoprotein complexes (nonpolar)
-cholesterol: transported in lipoprotein complexes (nonpolar) HDL and LDL
Back
Solution
Front
completely homogenous mixture, diffused solute in solvent
Back
Saturated fat
Front
single bonds between all carbons in fatty acid (i.e. saturated with hydrogen), solid at room temperature
Back
What does transport in blood depend on?
Front
Solubility
Back
Explain the structure of β-D-glucose
Front
Back
5 other necessary elements for life
Front
Sulfur: found in 2 amino acids
Calcium: chemical messenger that helps regulate cell processes
Phosphorus: ATP and DNA, RNA (phosphate)
Iron: needed in cytochromes for electron transport chains, hemoglobin
sodium: water balance/homeostasis, pumped into cells for water uptake, nerves
Back
Adhesion
Front
H bonds holding molecules to another substance
Back
Explain the structure of ribose
Front
Back
Covalent bonds
Front
sharing pair of valence electrons, # of electrons required to complete an atom's valence shell determines how many bonds will form
Back
What is the function, structure, and importance of structure and function together of cellulose?
Front
Function: structural material (plant cell walls)
Structure: chain of beta glucose with alternating bond orientations, gives strength (to build strong cell walls)
F&S: stacked, linear model, stronger, not soluble, good for structure, not digestable
Back
What 2 things can the many properties of water be attributed to?
Front
Its polarity and hydrogen bonds
Back
High boiling point
Front
Water has a boiling point of 100°C
Back
Polysaccharides
Front
Multiple monosaccharides bonded covalently
Back
High specific heat
Front
(Amount of heat absorbed)/(amount of heat lost/change temperature by 1°C)
(1 cal)/(g/°C)
Back
Monounsaturated fats
Front
have only one double bond
Back
Hydrolisis
Front
bonds between monomers are broken by adding water (digestion)
Back
Compound
Front
2 or more elements combined in a fixed ratio
Back
Inorganic
Front
Not consisting of or deriving from living matter.
Back
Catabolism
Front
breakdown of complex molecules into simpler molecules (ex. digestion, respiration)
Back
What is the function, structure, and importance of structure and function together of glycogen?
Front
Function: energy storage in animals (esp. in liver and muscles)
Structure: more highly branched alpha glucose
F&S: quick release needed, must be branched
Back
Compare the properties of water vs. methane (think thermal properties)
Front
Water has almost 2x the specific heat capacity of methane, water heat of vaporization is almost 3x that of methane, melting and boiling points of methane are lower than water
Back
Lipids
Front
Fats, phospholipids, steroids, waxes
All lipids are hydrophobic
Back
List the cohesive properties of water
Front
Cohesion, surface tension
Back
High heat of vaporization
Front
quantity of heat required to convert 1g from liquid to gas states (Evaporative cooling/sweat)
Back
Hydrogen bond
Front
Attraction (weak) between a partially positive H atom of one polar molecule and a partially negative atom (O or N) of another polar molecule
Bond between bases pairs in DNA
Back
Why is carbon important?
Front
Tetravalent (can form 4 covalent bonds), which allows it to produce a variety of stable organic compounds
Back
Name the most frequent elements in life
Front
CHON (Carbon, hydrogen, oxygen, nitrogen, and are main elements found in organic molecules in organisms)
Back
Nonpolar covalent bonds
Front
Electrons shared equally
Back
Surface tension
Front
Measurement of the difficulty to break or stretch the surface of a liquid
Back
Metabolism
Front
web of all enzyme-catalyzed reactions in a cell or organism
Back
List the thermal properties of water
Front
High specific heat, high heat of vaporization, and high boiling point
Back
Unsaturated fat (oils)
Front
contain double bonds between carbons in fatty acid
Back
Condensation reaction/dehydration synthesis
Front
Joins monomers: one monomer provides a hydroxyl group while the other provides a hydrogen to form a water molecule, which is removed.
Back
Cohesion
Front
H bonds holding water molecules together
Back
Organic
Front
Carbon compounds found in living organisms, almost all carbon compounds are organic
Back
What is the structure of Fats/Triglycerides?
Front
1 glycerol condensed with 3 fatty acids nonpolar C-H bonds in fatty acid "tails"
Back
Anabolism
Front
synthesis of complex molecules from simpler molecules (ex. making DNA, photosynthesis)
Back
Polymers
Front
3 or more covalently bonded monomers (subunits)
Back
Ionic bonds
Front
one atom strips valence electrons from another atom (high electronegativity difference), electron transfer creates ions (charged atoms)
Back
Falsification of Vitalism
Front
When urea (organic compound in liver) was artificially synthesized by German chemist Friedrich Wöhlerfor the first time, vitalism was deemed false.
Back
Disaccharides
Front
covalent bonds between 2 monosaccharides
formula=C12H22O11 (because a water molecule is lost in dehydration synthesis)
Examples:
-sucrose=glucose and fructose (transported by phloem in plants)
-maltose=glucose and glucose
-lactose=(milk sugar) glucose and galactose
Back
Polar covalent bonds
Front
One atom more electronegative than the other (creates partial charges)
Back
Vitalism
Front
The belief that living organisms possess a non physical inner force or energy that gives them the property of life
Back
What is the function, structure, and importance of structure and function together of starch?
Front
Function: energy storage in plants
Structure: chain of alpha glucose with same bond orientation
Amylose=unbranched
Amylopectin=branched (though less than glycogen)
F&S: flat, too big to dissolve
Back
Explain the structure of ⍺-D-glucose
Front
Back
What are the different types of unsaturated fats?
Front
Monounsaturated, polyunsaturated, cis, and trans
Back
List the solvent properties of water
Front
-water is a very good solvent, sometimes called the "universal solvent"
-substances that are able to dissolve in water are polar or ionic
Back
Section 2
(42 cards)
Explain the temperature graph of an enzyme
Front
Back
Explain the pH graph of an enzyme
Front
Back
Body Mass Index (BMI)
Front
BMI=(weight in kg)/(height in m^2)
metric
Back
Induced fit model
Front
Enzyme and substrate fit together, but enzyme conforms to substrate
Back
Give examples of protein utilization in industry
Front
Proteins produced by cultured cells in fermenters are used in:
-foods
-pharmaceuticals
-other products (enzymes in cleaning agents etc.)
Back
Noncompetitive inhibition
Front
Inhibitor binds to another part of the enzyme (allosteric site) altering its conformation (shape); ex. heavy metal poisoning (heavy metals bind to allosteric sites on enzymes)
Back
List the purposes of proteins (general)
Front
structure, transport, muscle contraction, defense, cell adhesion, tensile strengthening, DNA packaging, hormones, receptors, catalysis (enzymes), etc.
Back
Peptide bonds
Front
covalent bonds (carboxyl group to amino group)
Back
What are the four levels of structure in a protein?
Front
Primary, secondary, tertiary, and quaternary
Back
Trans fats
Front
hydrogen atoms on opposite sides of the double bond (produced by artificial partial hydrogenation of oils, no bend in fatty acid), solid at room temperature
Back
Cis fats
Front
hydrogen atoms on same side of double bond (typical natural isomer bend in fatty acid), liquid at room temperature
Back
Proteome
Front
All proteins produced by a cell, tissue, or organism at any given time
Every individual has a unique proteome (exception: identical twins, but become different as they age)
Back
Activation Energy
Front
Amount of energy necessary to start a reaction (energy required to break bonds in reactions)
Back
Secondary structure
Front
Coils and foils (due to hydrogen bonds at regular intervals), Alpha helix causes coiling (ex. keratin), pleated sheet is parallel (ex. silk)
Back
Explain the substrate graph
Front
Back
Denaturation
Front
Structural change in a protein that results in the loss (usually permanent) of its biological properties
Back
Phospholipids
Front
structure same as fat except 2 fatty acid tails and a phosphate group attached to glycerol
Back
How immobilized enzymes are used in industry (some examples, as well)
Front
-easy to separate from product
-can reuse enzymes
-can have higher enzyme concentrations
-increases enzyme stability
-ex. Lactase
Lactase obtained from cultured kluyveromyces lactis, a yeast that grows in milk
a) added to milk
b) immobilized on a surface or in beads of porous material (alginate beads)
Back
How do enzymes control metabolic pathways?
Front
Chains and cycle of enzyme, catalyzed reactions; ex. Cellular respiration - glycolysis: a chain, krebs cycle
Back
Give an example of enzyme inhibition in medicine
Front
ex. Ethanol is used as competitive inhibitor for alcohol dehydrogenate to treat antifreeze poisoning
Back
Quaternary structure
Front
2 or more polypeptide chains aggregated into 1 macromolecule (ex. collagen (connective tissue), hemoglobin)
Back
Active Site
Front
Pocket or groove on an enzyme that binds to substrate (i.e. the spot on the enzyme where reaction occurs)
Back
Explain the graph of the effects of inhibition on enzyme kinetics
Front
Look at the top graph
Back
Polyunsaturated fats
Front
more than one double bond
Back
List the purposes of lipids
Front
long term storage, more energy/gram (lighter energy storage), insoluble in water so they don't cause problems with osmosis
Back
Polypeptides
Front
formed by condensation reaction, multiple amino acids
Back
What are the four parts surrounding a central carbon in an amino acid?
Front
1) amino group (NH2)
2) carboxyl group (-COOH)
3) H atom
4) variable groups (determine the amino acid's properties, ex. polar (hydrophilic), nonpolar (hydrophobic), acid, or base)
The only part that varies is the R-group
Back
Coenzyme
Front
Organic helpers (ex. vitamins)
Back
End product inhibition/Feedback inhibition
Front
The end product of pathway acts as an inhibitor for an enzyme in the pathway, thus slowing it down.
wide range of functions, each has a complex 3-D shape (conformation), monomers are amino acids (there are 20)
Back
Competitive inhibition
Front
Inhibitor competes for active site, mimics substrate (ex. Penicillin and enzyme for cell wall synthesis in bacteria)
Back
Enzymes
Front
Catalytic proteins that change the rate of reactions w/o being consumed; they lower activation energy
Back
What is enzyme inhibition?
Front
An inhibitor stops the substrate from reaching the active site
Back
Steroids
Front
lipids with 4 fused carbon rings
Example: Cholesterol
-used in cell membranes
-precursor for other steroids (sex hormones)
-atherosclerosis
Back
What is the general formula for saturated fats?
Front
COOH-(CH2)n-CH3
Back
Substrate
Front
Enzyme reactant
Back
List the purposes of carbohydrates
Front
short terms storage, easier to digest (more rapid energy release), soluble in water (easier to transport in blood etc.), 4 calories/gram
Back
Tertiary structure
Front
Overall 3D shape of the polypeptide
Contortions from R-group bonding
-hydrophobic interactions (nonpolar side chains)
-disulfide bridges (strong covalent bonds)
-hydrogen bonds (between polar side chains)
-ionic bonds (charged side chains)
Back
Primary structure
Front
Order of amino acids, each type of protein has a unique primary structure, sequence determines 3D conformation
Amino acid substitution: hemoglobin, sickle-cell anemia
Back
Give examples of functions of specific proteins
Front
-Rubisco=carbon fixation during photosynthesis
-Insulin=hormone that regulates blood sugar by signaling glucose uptake by cells
-Immunoglobulins (antibodies)=specific immunity
-Rhodopsin=pigment that absorbs light in rod cells of retina
-Collagen=forms strong mesh of fibers in body (skin, blood, vessel walls, ligaments, bones, etc.)
-Spider silk=strong fibers for forming webs
Back
List the purposes of fats
Front
energy storage, organ cushioning, and thermal insulation