chap. 2 Flashcards

(60 cards)

1
Q

macromolecule sizes (smallest to biggest)

A

1) monomer
2) dimer (2 monomers)
3) oligomer (3-10 monomers)
4) polymer (11+ monomers)

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2
Q

Dehydration synthesis

A
  • binds a monomer to another macromolecule
  • one macromolecule loses an H atom, and the other loses an OH, the two bind together and produce a water molecule as a product
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3
Q

hydrolysis

A

adding water breaks bonds between monomers

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4
Q

what are the four types of macromolecules

A

carbohydrates, lipids, proteins, nucleic acids

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5
Q

functional groups

A

small groups of atoms that give properties/functions to the macromolecule

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6
Q

carboxyl groups make compounds…

A

make compound weak acids

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7
Q

amino groups make compounds…

A

make compounds weak bases

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8
Q

carbohydrates

A

AKA sugars
- carbon chain with 2 H for every 1 O
- near immediate energy use & short to medium term energy storage

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9
Q

carbohydrate sizes

A

monomers: monosaccharides
dimers: disaccharides
oligomers: oligosaccharides
polymers: polysaccharides

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10
Q

Lipids

A

AKA fats
- lots of C and H, few O

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11
Q

types of lipids and their functions

A

fatty acids: long term energy storage (monomer name)
phospholipids: form cell membrane
steroids: hormone (signaling membranes)

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12
Q

Nucleic Acids

A

composed of nucleotides
- store genetic informations
- immediate energy use
- includes DNA and RNA

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13
Q

ATP

A
  • adenosine triphosphate
  • nucleotide
  • immediate energy release in cells
  • breaking bonds of ATP = energy release
  • body uses 88lbs of ATP per day
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14
Q

Nucleotide

A
  • monomer of nucleic acids
  • made of a nitrogenous base, 5-carbon sugar (ribose or deoxyribose), and a phosphate group(s)
    more phosphates = more energy

example: ATP

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15
Q

Proteins

A

AKA polypeptides
- composed of amino acids
functions: structure, cell signaling, movement, protection, catalysis, etc

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16
Q

amino acids

A

monomer of proteins

made of a central carbon, amino group (NH2) which is a weak base, a carboxyl group (COOH) which is a weak acid, and a functional group (R-group) which determines the amino acid’s name and function

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17
Q

how are amino acids bound together?

A

polypeptide chains (aka peptide bonds)

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18
Q

how are peptide bonds formed

A

formed by dehydration synthesis reaction of COOH and NH2 group of respective amino acids

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19
Q

primary protein structure

A

sequence of amino acids, determines all other levels of structure

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20
Q

secondary protein structure

A

partial-folded structures
containing Alpha helices and Beta pleated sheets

caused by hydrogen bonds between amino acids

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21
Q

tertiary protein structure

A
  • 3D shape
  • shape determine the protein function
  • caused by interactions between R groups
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22
Q

conformation change

A

a change in protein function
- can be caused by different molecules binding, unbinding
- some proteins only function correctly when they undergo conformational changes regularly

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23
Q

denaturation

A

if a protein unfolds, losing its tertiary structure due to heat or acid exposure, it loses its function

denaturation is permeant

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24
Q

Quaternary Protein Structure

A

combination of two different polypeptides

caused by interactions between two polypeptides

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25
enzymes
- a class of protein - make reactions happen faster - very powerful and have lots of energy - lower activation energy: initial energy needed for a chemical reaction to occur
26
how enzymes work
enzymes have 3D activation sites that binds to a specific substrate when they bind it creates a "enzyme-substrate complex". They are not chemically bonded, just stuck together when the product is created in can not stay attached
27
Cell size
cells are small because they need a high surface area to volume ration the bigger a cell gets the smaller that ratio becomes
28
phospholipids
- forms 79% of the plasm membrane - hydrophilic heads on either side and hydrophobic tails on the inside (makes a bilayer)
29
glycolipids
a subtype of phospholipids but with a carbohydrate attachment
30
hydrophilic head
love water polar made of glycerol and phosphate
31
hydrophobic tail
hates water non-polar made of 2 fatty acids
32
cholesterol
spread out among the phospholipids making up about 19% of the membrane affects membrane fluidity (everything is constantly moving in the membrane) low cholesterol = stiff high cholesterol = fluid
33
plasma membrane proteins
- proteins embedded between phospholipids (making up 2% of the membrane) - there are many types and functions - include glycoproteins
34
glycocalyx
- carbohydrates extending off cell membrane - formed by glycoproteins and glycolipids - provides protection and identification (like a name tag) - if a cell shows up with the wrong glycocalyx, the immune system will get rid of it
35
type of plasma membrane proteins
receptors, channel proteins, and carrier proteins
36
receptor proteins
- binds to ligands - allows cellular communication/signaling - when a ligand binds, leads to the release if many other (secondary) messenger molecules inside the cell, greatly increasing the effect
37
ligands
any chemical used for signaling/communication
38
channel proteins
proteins with a passage allowing smaller molecules in/out of the cell Passive transport two types: leak channels (always open), and gated channels
39
gated channels
can be opened or closed by a stimulus 3 types: ligand gated, voltage gated, and mechanical gated
40
ligand-gated
opened/closed when the bind to a ligand
41
voltage-gated
open/closed when charge across membrane changes
42
mechanical-gated
open/close due to physical forces
43
carrier protein
transport proteins that CARRY smaller molecules across plasma membrane how it works: 1) molecule binds to site within carrier 2) carrier protein changes conformation (its tertiary structure) 3) molecule is released to other side of membrane
44
pumps
carrier proteins that require ATP to move molecules up gradient primary active transport
45
sodium-potassium pump
pumps out 3 Na+ and pumps in 2 K+
46
types of pumps
uniporters: move one type of molecule co-transporter: move two types of molecules - symporters: move 2 molecules same direction - antiporters: move 2 molecules in opposite directions
47
why are cell membranes semipermeable
so cells can maintain homeostasis - permeable to nutrients and wastes - impermeable to proteins and many charged ions
48
types of membrane transport
passive: simple diffusion, facilitated diffusion, and osmosis active: primary and secondary active transport
49
simple diffusion
- movement of molecules directly through phospholipids (no proteins needed) - lipids and gasses can pass directly through phospholipid bilayer
50
facilitated diffusion
movement of molecules down their gradient using carrier proteins or channel proteins - ions, polar, water, etc. need to use a protein
51
52
osmosis tonicity
the ability for a solution to affect the water volume of a cell
52
osmosis
water moves from an area of low solute (high water) concentration to an area of high solute (low water) concentration through aquaporin channel proteins *water wants to go where there is LESS water (high solute)*
53
hypotonic solution
has lower solution concentration than intercellular fluid water enters cell
54
hypertonic solution
has greater solution concentration than intercellular fluid water leaves cell
55
isotonic solution
has equal solute concentration as intercellular fluid no net fluid movement
56
active transport
membrane transport requiring carrier proteins and energy from ATP moves molecules up their gradient
57
primary active transport
movement of molecules using ATP directly
58
secondary active transport
movement of molecules using energy from ATP indirectly done by co-transporters molecule A moves down its concentration gradient, powering the movement of molecule B up its concentration gradient molecule A's concentration gradient is created by a primary active transporter
59
SGLT
- type of secondary active transport - moves sodium and glucose into the cell - sodium moves down concentration gradient, and glucose moves up - sodium has a concentration gradient because the Na-K Pump uses ATP to pump it out of the cell