IB Biology - Molecular Biology

IB Biology - Molecular Biology

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Density property of water

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Last updated

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Date created

Mar 1, 2020

Cards (92)

Section 1

(50 cards)

Density property of water

Front

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.

Back

Cofactors

Front

Inorganic, nonprotein helpers (ex. zinc, iron, copper)

Back

Proteins

Front

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

Back