Chapter 3 Protein Structure and Folding Flashcards

(53 cards)

1
Q

20 distinct building blocks of proteins (actually 22)

A

amino acids

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2
Q

the central carbon on an amino acids binds to these 4 structures:

A

H - hydrogen atom
NH2 - amino functional group
COOH - carboxyl group
distinctive “R” group, or side chain

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3
Q

in water, amino acids…

A

ionize

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4
Q

in water, the carboxyl group on an amino acid…

A

acts as an acid

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5
Q

in water, the amino group on an amino acid…

A

acts as a base

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6
Q

what makes the 20 amino acids unique from each other? Why?

A

the distinct R group, or side chain

it causes variation in properties

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7
Q

properties of polar and electrically charged R groups:

A

interact readily with water and are hydrophilic, dissolve readily in water

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8
Q

properties of non-polar R groups:

A

lack highly electronegative atoms capable of reacting with water
hydrophobic, coalesce in aqueous solution instead of dissolving

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9
Q

if the R group has a negative charge:

A

it is acidic and will lose a proton

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10
Q

if the R group has a positive charge:

A

it is basic and will pick up a proton

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11
Q

building blocks of polymers

A

monomers

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12
Q

if the R group is uncharged
A. with an oxygen
B. without an oxygen

A

A. the electronegative oxygen will form a covalent bond within the R group, making it an uncharged polar amino acid
B. its a non polar amino acid

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13
Q

meaning of monomer

A

one part

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14
Q

macromolecules

A

large molecules made up of smaller molecule subunits joined together, made up of monomers

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15
Q

monomers linking together:

A

polymerization

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16
Q

amino acids are the ______ that polymerize to form _____

A

monomers, proteins

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17
Q

monomer in, water out, occurs in a ________ reaction

A

condensation

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18
Q

water in, monomer out, occurs in a ________ reaction

A

hydrolysis

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19
Q

monomers polymerize through what type of reaction?

A

condensation reactions/dehydration reactions

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20
Q

polymerization

A

bonding together of monomers

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21
Q

bond between the amino group and the carboxyl group of two acids

A

peptide bond

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22
Q

R group orientation in the peptide backbone:

A

the R groups extend out from the back bone, can react with other R groups and water

23
Q

directionality in the peptide backbone:

A

amino group on one end (N terminus), carboxyl group on one end (C terminus)

24
Q

flexibility in the peptide backbone:

A

the bond on either side of the peptide bond can rotate, so the molecule is flexible

25
polymer with less then 50 amino acids
oligopeptide, or peptide
26
oligopeptide
few peptides
27
polymer with mire than 50 peptides
polypeptides
28
polypeptides
many peptides
29
proteins are ____ made up of _________
proteins are polymers made up of amino acids
30
Primary structure of proteins is determined by ____ and ______
peptide bonds and the unique sequence of amino acids that make up the protein
31
Changes in primary structure affect:
protein function
32
Types of bonds that support secondary structure?
hydrogen bonds
33
two possible secondary structures:
alpha helicies and beta pleated sheets
34
a proteins 3 dimensional shape is determined by its:
tertiary structure
35
5 types of bonds that affect tertiary structure
1. hydrogen bonding 2. hydrophobic interactions 3. van der waals interactions 4. covalent bonding (disulfide bonds) 5. Ionic Bonding (between charged groups)
36
A combination of polypeptide subunits results in:
quaternary structure
37
macromolecular machines
groups of multiple proteins that assemble to carry out a function
38
dimer
protein consisting of 2 identical polypeptide subunits
39
tetramer
protein consisting of 2 sets of identical polypeptide subunits
40
how are folding and function related? what happens when a protein is denatured?
folding is crucial to function, denaturing a protein breaks disulfide and hydrogen bonds and keeps proteins from working properly
41
which proteins facilitate protein folding?
molecular chaperones
42
do proteins only have one shape?
no, proteins are somewhat flexible and dynamic, until they are prompted into their functional form
43
Stanley Prusiner on protein folding
some proteins are induced to fold into disease causing , infectious agents called prions
44
side effect of prions in several mammals
brain degeneration
45
proteins that catalyze are called:
enzymes
46
proteins that attack and destry viruses are called:
antibodies
47
_____ _______ are responsible for the movement of the cell, and moving large molecules within the cell
motor proteins
48
proteins are involved in ________ from cell to cell around the body
carrying and receiving signals
49
_______make up body component like skin and nail and form the internal skeleton of cells
structural proteins
50
catalyzed reactions involve one or more reactants called :
substrates
51
enzymes hold substrates in the exact orientation...
to that they can react
52
Emil Fischer's idea
lock and key model of enzymes and substrates
53
where substrates bind to enzymes is the:
active site