1. Chemistry + Flashcards

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1
Q

Properties of H2O

A
  1. great solvent.
  2. high heat capacity. must add a lot of energy to warm.
  3. Ice floats. H2O becomes less dense as it freezes.
  4. Cohesion/surface tension. attraction btw like subst. H bonding.
  5. Adhesion. attraction of unlike substances; capillary action: ability of liquid to flow w/o external forces (against gravity).
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2
Q

Monosaccharids

A
  • single sugar molec. (ex. glucose, fructose, galactose).

- alpha or beta based on position of OH on first anomeric C. (down = alpha, up= beta).

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3
Q

Disaccharide

A
  • two monosaccharides joined by glycosidic linkage (joined by dehydration).
  • Sucrose = glucose + fructose
  • lactose = glucose + galactose
  • maltose = glucose + glucose
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4
Q

Polysaccharide

A
  • series of connected monosaccharides, polymer.

- bond via dehydration synthesis, breakdown via hydrolysis.

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5
Q

Starch

A
  • polymer of alpha glucose

- energy storage in plant cell

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6
Q

Glycogen

A
  • polymer of alpha glucose

- energy storage in animal cells

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7
Q

Cellulose

A
  • polymer of beta glucose

- plant cell walls

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8
Q

Chitin

A
  • polymer similar to cellulose but each beta glucose has a N-containing group attached to ring
  • fungal cell walls (also exoskeleton of insects)
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9
Q

Lipids

A
  • hydrophobic molecules
  • functions: insulation, energy storage, structural (cholesterol and phospholipids), endocrine
  • triglycerides, phospholipids, steroids
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10
Q

Triglycerides

A
  • 3 fatty acid chains attached to a glycerol backbone
  • saturated: no double bonds, bad for health, stack densely and form fat plaques
  • unsaturated: double bonds, stack less dense
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11
Q

Phospholipids

A
  • two fatty acids and a phosphate group attached to a glycerol backbone
  • amphipathic = both hydrophobic and hydrophilic
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12
Q

Steroids

A
  • three 6 membered rings and one 5 membered

- hormones and cholesterol (membrane component)

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13
Q

Lipid Derivatives

A
  • phospholipids
  • waxes: esters of fatty acids and monohydroxylic alcohols
  • steroids: sex hormones, cholesterol
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14
Q

Carotenoids

A
  • fatty acid carbon chains w/ conj double bonds and six membered C-rings at each end.
  • pigment that produces colors in plants and animlas
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15
Q

Porphyrins (tetrapyrroles)

A
  • 4 joined pyrrole rings

- often complex w/ metal. (porphyrin heme complexes w/ Fe in hemoglobin, chlorophyll w/ Mg)

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16
Q

Adipocytes

A
  • specialized fat cells
  • white fat cells: large lipid droplet, primarily triglycerides w/ small cytoplasm around it.
  • brown fat cells: considerable cytoplasm, lipid droplet scattered throughout, and lots of mitochondria
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17
Q

Glycolipids

A
  • like phospholipids but w/ carb group instead of phos.

- note: lipids are insoluble so they are transported in blood via lipoproteins

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18
Q

Lipids in membranes

A
  • fluid

- in cold weather, to avoid rigidity, cells incorporate more mono and polyunsaturated fatty acids (lower m.p.)

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19
Q

Proteins

A
  • polymers of amino acids joined by peptide bonds
  • storage, transport (hemoglobin carries O2, cytochromes carry e-), enzymes (amylase catalyzes breaking a-glycosidic bonds in starch
20
Q

Amino Acid Structure

A
  • amino group, carboxylic acid group, and a variable side chain bonded to a central C
21
Q

Enzymes

A
  • protein catalyst
  • ex. amylase (catalyze breaking a-glycosidic bonds in starch.
  • catalyzes both the forward and reverse rxns.
  • cannot change spontaneity of a rxn.
  • enzymes are almost always proteins, but sometimes RNA can act as an enzyme (riboenzyme)
22
Q

Cofactors

A
  • nonportein molec. that assist enzymes
  • holoenzyme is union of cofactor and enzyme
  • enzyme is apoenzyme/apoprotein when not bound to cofactor
  • organic -> coenzyme, ex. vitamins
  • inorganic -> metal ions, Fe +2, Mg+2,
  • prosthetic group -> cofactor strongly bound to enzyme
23
Q

Different Structures of a Protein

A
  • primary: amino acid sequence
  • secondary: 3d shape, H bonding btw amino and carboxyl groups, alpha helix, beta sheet
  • tertiary: 3d due to noncovalent interactions, H bond, ionic, hydrophobic, disulfide bonds, van der walls.
  • quaternary: grouping of two or more separate peptide chains.
24
Q

Three Protein Categories

A
  1. Globular: somewhat H2O soluble, many functions, enzymes, hormones, storage & transport, osmotic regulation, immune response, etc., mostly dominated by 3ary structure
  2. Fibrous/stuctural: not H2O soluble, long polymers, maintain strength of cellular and matrix structure, mostly dominated by 2ary structure.
  3. Membrane proteins: membrane pumps/channels/receptors
    - Note: protein denaturation means 2ary structure onward is removed, not necessarily that the protein itself is broken down into amino acids.
25
Q

Nucleotide

A
  • Nitrogen base, 5-C sugar, phosphate group
26
Q

Nucleoside

A
  • Sugar + Base
27
Q

Purines

A
  • Adenine and Guanine

- 2 rings

28
Q

Pyrimidines

A
  • Thymine, Cytosine, Uracil

- 1 ring

29
Q

DNA

A
  • polymer of nucleotides that contain deoxyribose
30
Q

RNA

A
  • polymer of nucleotides that contain ribose, not deoxyribose
  • Thymine replaced by uracil
  • usually single stranded
31
Q

Cell Doctrine/Theory

A
  1. all living organisms are composed of one or more cells
  2. cell is the basic unit
  3. cells come from preexisting cells
  4. cells carry hereditary information
32
Q

RNA World Hypothesis

A
  • self-replicating RNA molecules were precursors to current life
  • RNA carries genetic info and can catalyze chemical reactions
  • RNA is unstable compared to DNA, so more likely to participate in chemical rxns (due to extra OH group)
33
Q

Central Dogma of Genetics

A

DNA -> RNA -> Protein

34
Q

Stereomicroscope

A
  • visible light for surface of sample

- can look at living samples, but low resolution

35
Q

Compound Microscope

A
  • visible light for thin section of sample
  • can look at some living samples (single cell layer),
  • may require staining
36
Q

Phase Contrast

A
  • uses light phases and contrast
  • allows for detailed observation of living organisms
  • good resolution/contrast but not good for thick samples
37
Q

Confocal laser scanning + fluorescence

A
  • can look at thin slices while keeping sample intact
  • can look at specific parts of cell via fluorescent tagging
  • can look at living cells, but only fluorescently tagged parts
  • used to observe mitosis
  • can be used w/out fluorescence
38
Q

Scanning Electron Microscope

A
  • look at surface of 3D objects w/ high resolution

- can’t use on living

39
Q

Transmission Electron Microscope

A
  • look at thin cross-sections in high detail
  • can look at internal structures
  • very high resolution
  • can’t be used on living things
40
Q

Electron Tomography

A
  • 3D model buildup using TEM data
  • can look at objects in 3D and see objects relative to one another
  • can’t be used on living things
41
Q

Centrifugation

A
  • spins + separates into layers based on density.
  • most dense/fastest to pellet out the bottom is nuclei layer, spin faster -> mitochondria/chloroplasts/lysosomes. peroxisomes, spin faster -> microsomes/small vesicles, then ribosomes, viruses, larger macromolec
42
Q

Allosteric Enzyme

A
  • both an active site for substrate binding and an allosteric site for activator/inhibitor
43
Q

Competitive Inhibition

A
  • substance that mimics the substrate inhibits the enzyme by binding at active site
  • can be overcome by increasing subs conc
  • km raised, but Vmax is unchanged
44
Q

Noncompetetive Inhibition

A
  • substance inhibits enzyme by binding elsewhere than active site
  • substrate still binds but rxn is prevented from completing.
  • km unchanged, Vmax is not
45
Q

Cooperativity

A
  • enzyme more receptive to additional substrate binding after one substrate molecule attaches to active site.
  • ex: hemoglobin binding to O2, although hemoglobin is not an enzyme
46
Q

Michaelis Constant (Km)

A
  • substrate conc at which rate is 1/2 Vmax
  • small Km indicates enzyme requires only small amount of substrate to become saturated
  • raised Km = substrate binding worse
  • lowered Km = substrate binding better