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intro cell + molec bio > day 3 > Flashcards

day 3 Flashcards

1
Q

4 parts of an amino acid

A

amino group
side chain (R)
carboxyl group
alfa carbon

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2
Q

what bonds exist with a non-polar side chain (R)

A

london forces + hydrophobic interactions

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3
Q

what bonds exist with an UNCHARGED polar side chain (R)

A

hydrogen bonds + hydrophylic interactions + london forces

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4
Q

what bonds exist with a CHARGED polar side chain (R)

A

electrostatic attraction + hydrophylic interactions + hydrogen bonds + london forces

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5
Q

true/false: polypeptide chains (proteins) have directionality

A

TRUE

always have an amino group on one end (n-terminus) and a carboxyl group on the other end (c-terminus)

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6
Q

c-terminus

A

carboxyl group on end of polypeptide chain. new amino acids are added to this end of the chain

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7
Q

n-terminus

A

amino acid group on end of polypeptide chain. first amino acid that started the chain (new amino acids added to c-terminus)

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8
Q

primary structure

A

a sequence of amino acids linked by peptide bonds. always in the N-C-C order

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9
Q

secondary structure

A

local regions of polypeptide chains form 3D shapes. either alfa helix or beta sheet. formed by backbone interactions

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10
Q

2 types of secondary structures formed

A

alfa helix + beta sheet

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11
Q

tirtiary structure

A

final folding of polypeptide innitiated/involves mostly side chain (R) interctions

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12
Q

quaternary structure

A

only in multimeric proteins, the association between 2 or more peptides as they interact to form the final and functional protein

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13
Q

alfa helix formation

A

formed by hydrogen bonds between oxygen and hydrogen from seperate amino acids four units away on primary backbone

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14
Q

beta sheets

A

hydrogen bonds between oxygen + hydrogen on the primary backbone from adjacent regions forming rows (antiparallel or parallel)

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15
Q

chaperones

A

chaperones make polypeptide folding more efficient and reliable

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16
Q

2 ways chaperones work

A
  1. binding to partially folded chains
  2. form folding chambers
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17
Q

conformation

A

final 3D shape of polypeptide chain. determined by interactions between amino acids that forms the lowest free energy state

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18
Q

what 3 components can make up a tirtiary structure?

A

alfa helixes, beta sheets, random coils/unstructured regions

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19
Q

domain

A

segment of a polypeptide chain that folds into discrete and stable structure.

NOT the same as multimeric proteins

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20
Q

multimeric proteins

A

proteins made from more than one polypeptide chain which form ONE final functional protein

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21
Q

ligand

A

any substance bound by protein at a specific binding site

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22
Q

antibodies

A

bind antigens (ligands) at the interface of the heavy and light chains with high specificity

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23
Q

imunohistochemistry

A

detecting proteins (antigens) in cells or tissue using antibodies tagged with florescent labels.

demonstrates where a specific protein exists in a cell or tissue

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24
Q

substrate

A

ligand in an enzymatic reaction

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25
Q

active site

A

a pocket/grove in an enzyme with chemical + structural properties that accomodates the substrate (essentially the binding site for substrate)

26
Q

explain lock/key model and induced fit model

A

lock/key model: specific shape of substrate matched exactly with specific shape of active site on enzyme

induced fit model: the enzyme and substrate mold around eachother to fit perfectly (through electrostatic attraction/positive and negative charges) and then the enzyme returns to original form once products are formed

27
Q

conformational change

A

binding of the substrate to enzyme induces a conformational change in both enzyme and substrate that helps catalize rxn

28
Q

competitive enzyme inhibitors

A

substrate and inhibitor compete for the same active site (if inhibitor is there, substrate cannot bind and trigger a reaction)

29
Q

allsteric inhibition

A

there exists both an allosteric site and an active site. when the substrate binds to the active site, the products are produced, if allosteric site is filled with allosteric inhibitor the substrate does not fit and the reaction cannot occur. only one (either substrate or allosteric inhibitor can bind at once)

30
Q

allosteric activation

A

there exists both an allosteric binding site and an active site. when nothing is bonded to this molecule (no allosteric activator), the shape of the molecule is incorect and the substrate does not fit. when the allosteric activator binds to the allosteric site, the substrate can fit and the product is produced

31
Q

kinase

A

enzyme that adds a phosphate to a molecule (phosphorization)

32
Q

phosphatase

A

enzyme that removes a phosphate group (dephosphorylation)

33
Q

do fatty acids that make up membrain lipids make up polypeptide chains?

A

NO THEY DO NOT.

still a macromolecule though

34
Q

lipid functions

A

energy storage, membrain structure, chemical signaling

35
Q

types of lipids

A

fatty acids
tryglicorides
phospholipids
glycolipids
steroids
terpines

36
Q

fatty acid

A

long, unbranching hydrocarbon chain with a terminal carboxyl group

37
Q

saturated fat

A

no double bonds, written as straight squigly line. solid at room temperature + easy to stack.

38
Q

unsaturated fat

A

contains at least one double bond, written as straight squigly line with bend at the double bond. liquid at room temperature, harder to stack.

39
Q

three main types of membrain lipids

A

phosphatidylcholine (PC), cholesterol, glycolipids

40
Q

amphipathic

A

a molecule containing both hydrophobic and hydrophilic regons

41
Q

phosphatidylcholine (PC)

A

most common phospholipid in cell membranes

hydrophilic head:
choline group
phosphate group
glycerol group

hydrophobic tails:
hydrocarbon tail (2)

42
Q

cholesterol

A

packs between unsaturated fatty acid chains (polypeptides) to add rigidity to the membrain and reduce permiability

hydrophilic head:
polar head group (OH)

rigid planar steroid ring structure

hydrophobic tail:
hydrocarbon tail (1)

43
Q

glycolipids

A

have sugars (carbohydrates) exposed to the extracellular (outside) environment which serve as markers for cell recognition

44
Q

what ennzyme is used to ‘flip’ phopholipids from one side to the other

A

flippase

45
Q

flippase

A

uses energy from the hdrolysis of ATP to keep phosphatedylserine on the ‘inside’/cell side of the plasma membrane

46
Q

membrane organization and asymetry is organized where

A

the golgi aparatus – organized oppositly in golgi membrane, fliped when in real cell membrane

47
Q

aptosis

A

programmed cell death/intercellular death program

48
Q

what does phosphatidylserine (PS) signal when on the OUTSIDE of a cell membrane

A

EAT ME! (distroy me and recycle organelles etc inside)

49
Q

small non-polar molecules pass BLANK through the cell membrane

(O2, N2, CO2)

A

EASILY + QUICKELY

50
Q

small uncharged polar molicules pass BLANK through the cell membrane

(H2O, ethinol, glycerol)

A

LESS QUICKELY + EASILY (than small non-polar molecules)

51
Q

larger uncharged polar molecules pass BLANK through the cell membrane

(amino acids, glucose, nucleosides)

A

INFREQUENTLY (usually moved through by transport)

52
Q

ions pass BLANK through the cell membrane

(H+, Na+, K+, etc)

A

NEVER pass through cell membrain on their own (need help, atp)

53
Q

types of proteins imbedded in membrane (4)

A

transporters and channels
anchors
receptors
enzymes

54
Q

passive transport

A

molecules move with concentration gradient (still need help moving through channel for example but is still moving with concentration gradient so no ATP needed)

55
Q

active transport

A

molecules moving against concentration gradient. needs energy to drive movement against gradient, ATP

56
Q

simple difusion

A

freely moving through membrane (down conc. gradient)

57
Q

voltage gradient

A

difference in charge accross a membrain

58
Q

concentration gradient

A

difference in concentration accross a membrain

59
Q

electrochemical gradient

A

a combination of voltage and concentration gradients

60
Q

sodium/potassium pump

A

uses ATP to pump 3Na+ ions out and 2K+ ions in to maintain correct eletrochemical gradient across the cell membrane

61
Q

symport

A

moves 2 molecules at same time (one down its gradient, the other up) by using the energy released from the movement of one molecule down its gradient (ex. Na+) to simultaniously move the second molecule up its concentration gradient (ex. glucose)

intro cell + molec bio (14 decks)

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