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Phys > Chapter 2 > Flashcards

Chapter 2 Flashcards

1
Q

what do organic molecules contain?

A

carbon

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2
Q

what are biomolecules?

A

organic molecules living organisms

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3
Q

what are the four major groups?

A

carbohydrates, lipids, proteins, nucleotides

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4
Q

what do most molecules and bonds contain?

A

C, H, O, and N
N is the most common element on all proteins

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5
Q

basic functions of biomolecules

A

energy and building blocks

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6
Q

saturated fatty acids

A
  • no double bonds btw carbons, so they are saturated with hydrogens. the more saturated a fatty acid is the more likley it is to be solid at room temp
  • ex: animal fat
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7
Q

monosaturated fatty acids

A
  • one double bond btw two of the carbons in the chain. for each double bond, the molecule has two fewer hydrogen atoms attached to the carbon chain
  • liquid at room temp
  • ex: plant liquids
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8
Q

polyunsaturated fatty acids

A
  • two or more double bonds btw carbons in the chain
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9
Q

steroids

A
  • lipid-related molecules whose structure includes four linked carbon rings
  • cholesterol = steroid backbone
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10
Q

phospholipids

A
  • have two fatty acids and a phosphate group
  • cholesterol and phospholipids are important components of animal cell membranes
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11
Q

carbohydrates

A
  • brain feeds off of this
  • most abundant biomolecule
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12
Q

ribose

A
  • forms the sugar-phosphate backbone of RNA
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13
Q

deoxyribose

A
  • forms the sugar-phosphate backbone of DNA
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14
Q

fructose

A
  • found in fruit
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15
Q

glucose (dextrose)

A
  • found in any carbohydrate source
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16
Q

galactose

A
  • only found in milk
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17
Q

glucose + fructose

A
  • sucrose
  • disaccharide
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18
Q

glucose + galactose

A
  • lactose
  • disaccharide
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19
Q

glucose + glucose

A
  • maltose
  • disaccharide
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20
Q

glucose is in what?

A
  • in every disaccharide
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21
Q

polysaccharides

A
  • glucose polymers
  • all living cells store glucose for energy in the form of a polysaccharide
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22
Q

glycogen

A
  • giant chain of glucose
  • found in liver and muscles
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23
Q

peptide bond

A
  • how amino acids connect to one another
  • the amino group of one amino acid joins the carboxyl group of the other, with the loss of water
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24
Q

amino acids

A
  • links that form tgthr to form proteins
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25
Q

9 essential amino acids

A
  • arginine
  • asparatic acid (aspartate)
  • cysteine
  • glutamic acid (glutamate)
  • glutamine
  • glycine
  • tryptophan
  • tyrosine
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26
Q

where can all 9 essential amino acids be found?

A
  • in all meat and quinoa
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27
Q

homocysteine

A
  • a sulfur-containing amino acid that in excess is associated with heart disease
28
Q

y-amino butyric acid (gamma-amino butyric acid) or GABA

A
  • a chemical made by nerve cells
29
Q

creatine

A
  • a molecule that stores energy when it binds to a phosphate group
  • so you can lift more heavy weights
30
Q

primary structure

A
  • sequence of amino acids held tgthr by a peptide bond
  • peptides range in length from two to two million amino acids
  • oligopeptide: 2-9 amino acid
  • polypeptide: 10-100 amino acid
  • proteins: >100 amino acids
31
Q

secondary structure

A
  • created primarily by hydrogen bonds btw adjacent chains or loops
  • covalent bond angles btw amino acids determine secondary structure
  • alpha-helix
    > DNA double helix
    > single alpha helix: RNA
  • beta-strands form sheets
32
Q

tertiary structure

A
  • protein’s three dimensional shape
  • can be a mix of secondary structures
  • r groups bonding with one another
33
Q

quaternary structure

A
  • giving the protein a fxn
  • multiple subunits combine with noncovalent bonds
  • proteins bond with each other to form larger structures
  • ex: hemoglobin
34
Q

important cations of the body

A

Na+ = extracellular
K+ = intracellular
Ca2+
H+
Mg2+

35
Q

important anions of the body

A

Cl-
HCO-3 = bicarbonate (extracellular)
HPO-2 4 = phosphate (intracellular)
SO-2 4

36
Q

types of tertiary structure

A
  • globular proteins
  • disulfide bonds (S-S)
  • fibrous proteins
37
Q

why are molecular bonds critical?

A

critical in determining molecular shape

38
Q

enzymes

A
  • speed up chem rxn
39
Q

membrane transporters

A
  • help move substances back and forth btw intracellular and extracellular compartments
40
Q

receptors

A
  • proteins that bind signal molecules and initiate cellular responses
41
Q

binding proteins

A
  • bind and transport molecules
42
Q

immunoglobulins

A
  • protect the body from foreign invaders and substances
43
Q

regulatory proteins

A
  • turn cell processes on and off or up and down
44
Q

ligand

A
  • molecule or ion that binds to another molecule
  • ligand binding: requires molecular complementarity
45
Q

substrate

A

ligands that bind to enzymes and membrane transporters

46
Q

specificity

A
  • the ability of a protein to bind to a certain ligand or a group of closely-related ligands
47
Q

affinity

A
  • degree to which a protein is attached to a ligand
  • more binding sites = affinity goes down
48
Q

equilibrium

A
  • rate of binding is exactly equal to the rate of unbinding
  • equilibrium constant (Keg)
49
Q

What does water always follow in the body?

A

Na

50
Q

competitors

A

related ligands compete for the binding site

51
Q

agonists

A

competing ligands that mimic each others actions

52
Q

isoforms

A

closely-related proteins - function is similar but affinity for ligands differs

53
Q

How are proteins activated following transcription/translation?

A
  • posttranslational modification
  • peptide bonds are spliced btw exons and introns
  • cofactors like ions and small organic fxnal groups bind to the proteins affect how its folded and its functionality
54
Q

introns

A

taken out

55
Q

exons

A

expressed

56
Q

chemical modulators

A

bind reversibly or irreversibly to proteins and alter their binding affinity or activity

57
Q

competitive inhibitors

A

compete directly w ligand by binding reversibly to active sites

58
Q

irreversible antagonists

A

binds to binding site and cannot be displaced

59
Q

allosteric modulators

A
  • binds to protein away from binding site and changes activity
  • may be inhibitors or activators
60
Q

covalent modulators

A
  • binds covalently to protein away from binding site and changes its activity
61
Q

physical modulators

A
  • temp, pH
  • the body regulates the amount of protein in cells
  • up regulation: production of proteins
  • down-regulation: programmed removal of proteins
62
Q

reaction rate can reach a maximum

A
  • concentration of ligand = determines magnitude of response
  • saturation - maximum reaction rate (proteins are fully occupied)
63
Q

pH < 7

A

acidic

64
Q

pH > 7

A

alkaline

65
Q

look at page 19

A

LOOK AT IT

66
Q

look at page 20

A

LOOK AT IT

Phys (13 decks)

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