Molecules and Fundamentals of Biology Flashcards

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1
Q

Phosphatase

A

An enzyme that cleaves/removes a phosphate group off a substrate molecule

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2
Q

What does a large Km suggest?

A

large amount of substrate is needed because enzyme availability is low

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3
Q

Kinase

A

Enzyme that transfers a phosphate group from an ATP molecule to a substrate molecule, does NOT break bonds in order to add a phosphate group

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4
Q

What does a small Km suggest?

A

small amount of substrate is required because enzyme availability is high

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5
Q

How are molecules formed?

A

When two or more atoms join together
Ex: oxygen gas (O2)

joined together via interactions of electrons

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6
Q

How are compounds formed?

A

When two or more atoms of at least 2 different elements join together

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7
Q

During polymerization, what is added to the 3’ end of the sugar-phosphate backbone?

A

nucleoside triphosphate is added to the growing nuclei acid polymer by losing two phosphates as pyrophosphate, forming a phosphodiester bond with the free hydroxyl at the 3’ end of the polymer

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8
Q

Feedback regulation

A

When the end product of a reaction pathway negatively inhibits an upstream (earlier) enzyme

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9
Q

Biosynthetic reactions

A

Also known as anabolic reactions, convert substrates into more complex products in living organisms —> the products are more ordered and have a decreased entropy compared to their reactants

Example: photosynthesis converts solar energy into chemical energy - 6 carbon dioxide and water molecules produce fixed carbon in the form of glucose which is more complex and more ordered than water and carbon dioxide and has a decreased entropy compared to them

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10
Q

what type of bond are glycosidic bonds?

A

covalent bonds

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11
Q

what type of bonds are associated with tertiary structures of proteins?

A
  • Due to non-covalent interactions between R-groups
  • ionic bonding, hydrogen bonding, dipole-dipole interactions, london dispersion forces (Van der Waals forces) , hydrophobic interactions
  • disulfide bridges (strong covalent bond between cysteines, contributes to 3D structure)
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12
Q

what type of bonds are associated with primary structures of proteins?

A
  • primary structure are linear sequences of amino acids linked via peptide bonds (covalent bonds) that attach between one amino acids carboxyl group and the other amino acids amino group
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13
Q

waxes

A
  • lipid derivative
  • long fatty acid tails and monohydroxy alcohols joined together via ester linkages
  • provides a hydrophobic protective coat
  • ex: found on some plant leaf surfaces and some aquatic bird feathers
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14
Q

carotenoid

A
  • lipid derivative
  • long carbon chains with conjugated double bonds with 6-membered ring on each end
  • function as pigments, producing colors in plants and animals
  • ex: carotenoid cerotene gives the yellow to orange color and xanthophylls
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15
Q

porphyrins

A
  • (tetrapyrroles)
  • lipid derivative
  • comprised of four joined pyrrole rings that are often complex with a metal ion
  • ex: hemoglobin
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16
Q

brown fat cells

A
  • a type of adipocyte
  • contain a considerable amount of cytoplasm, lipid droplet scattered throughout, and lots of mitochondria
17
Q

white fat cells

A
  • a type of adipocyte
  • composed primarily of triglycerides with a small layer of cytoplasm around it
18
Q

Vmax is the:

A

maximal velocity of an enzyme

19
Q

globular proteins

A
  • water-soluble
  • dominated by tertiary structure
  • contain a diverse range of functionality: enzymatic, hormonal, inter/intracellular storage and transport, osmotic regulation and immune response
20
Q

what property of water makes it a good biological solvent?

A

waters polarity caused by dipoles of H2O break up charged ionic molecules, making it easy for water to dissolve substances

21
Q

what are the five important properties of water?

A

1) excellent biological solvent
2) high heat capacity
3) ice floats
4) cohesion/surface tension
5) adhesion

22
Q

adhesion propoerty of water:

A
  • water is attracted to unlike substances as well
  • ex: wetting finger to flip a page
  • has capillary action: the ability to flow without external forces
23
Q

cohesion/surface tension propoerty of water:

A
  • water is attracted to like substances due to its H-bonds
  • water has strong cohesion between other water molecules which produces high surface tension that allows for bugs to walk on water
24
Q

heat capcity property of water:

A
  • water has a high heat capacity
  • heat capacity: ability to change temperature in response to gaining/losing heat
  • water has stable temperatures in response to changes in surrounding temperatures, large amount of energy must be added to warm up water

heat capacity: changing temp. in response to gaining/losing heat

25
Q

ice floats propoerty of water:

A
  • water expands as it freezes
  • becomes less dense than its liquid form
  • due to H-bonds becooming rigid, forming a crystal that keeps the molecules separated
26
Q

glucose +fructose

A

sucrose

27
Q

glucose + galactose

A

lactose

28
Q

glucose + glucose

A

maltose

29
Q

celll theory:

A
  • all living organisms are composed of one or more cells
  • the cell is the basic unit of structure, function and organization in all organisms
  • all cells come from preexisting, living cells
  • cells carry hereditary information
30
Q

RNA world hypothesis

A
  • self-replicating RNA molecules were the precursors to current life
  • RNA stores genetic information like DNA
  • RNA catalyzes chemical reactions like enzymes
  • RNA played a major role in the evolution of cellular life
  • hypothesis recieved support from the fact that RNA is unstable compared to DNA due to extra OH group –> makes it likely to participate in chemical reactions
31
Q

fibrous/structural proteins

A
  • not water-soluble
  • dominated by secondary structure
  • made of long polymers
  • function to maintain and add strength to cellular and matrix structure
  • ex: collagen, keratin
32
Q

membrane proteins

A
  • proteins that function as membrane pumps, channels or receptors
33
Q

cofactors

A
  • non-protein molecules that assist enzymes
  • can be organic (vitamins) or inorganic (iron and magnesium)
34
Q

holoenzyme

A
  • union of a cofactor and an enzyme
35
Q

apoenzyme

A
  • when an enzyme is not combined with a cofactor
36
Q

coenzyme

A
  • an organic cofactor
  • ex: vitamins
37
Q

prosthetic group

A
  • a cofactor that is covalently bound to an enzyme
38
Q

simple proteins

A
  • formed entirely of amino acids
  • ex: albumin and globulins: functional proteins that act as carriers or enzymes
  • ex: scleroprotein: fibrous proteins that have structural function (collagen)
39
Q

conjugated proteins

A
  • simple protein + non-protein
  • lipoprotein: protein bound to lipid
  • mucoprotein: protein bound to carbohydrate
  • chromoprotein: protein bound to pigmented molecule
  • metalloprotein: protein complexed around metal ion
  • nucleoprotein: contains histone or protamine bound to nucleic acid