Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biopharmaceuticals Final > Module #2 - Biotargets of Drugs > Flashcards

Module #2 - Biotargets of Drugs Flashcards

(74 cards)

Start Studying
1
Q

what are the four main types of biological molecules

A

proteins
nucleic acids
polysaccharides
lipids (fats and steroids)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

describe simple/overall structure of proteins

A

linear chain of amino acids connected by amide (peptide) bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

describe structure of nucleic acids

A

linear chain of nucleotides connected by phosphate esters

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

describe structure of polysaccharides

A

linear chain of sugars, some branched

connected by acetals

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

describe structure of lipids

A

linear chains of acetate or propionate

connected by reduced aldol

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what is responsible for assembling and disassembling proteins

A

ribosomes assemble

proteasome disassemble

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

why are biological molecules modular?

A

fit together like building blocks

provide body with simple way to make lots of different molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

why is modular construction important?

A

allows for complex structures to be assembled using simple molecule components

allows for complex structures to be disassembled, and to regenerate parts to re-use

make living systems possible

only one enzyme system required for each biomolecule type and function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

how are proteins assembled

A

amino acids are linked together by ribosomes using amide (peptide bonds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

how are proteins disassembled

A

proteasome break apart the chains of amino acids (and the amide bonds between then)

protein is essentially broken down into individual amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what is the most common drug target in the body?

A

proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

how do drugs produce effects in the body?

A

bind to targets/receptors of biomolecules

results in biological change (ie. shape change)

results in biological response (

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

importance of 3D effect of biomolecules

A

allows biomolecules to bind and be recognized

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

why do drugs follow like-dissolves-like rule

A

drug will interact with biological molecules with similar chemical properties

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what is the general structure of an animo acid?

A

amine group (NH2)
acid group (COOH)
side chain (r)

all have same stereochemistry/backbones, but different side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

what are the five major classes of amino acids

A

nonpolar
acidic
basic
polar
special

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what is special about cysteine amino acid?

A

has R configuration at alpha carbon

sulfur has higher atomic number than oxygen, which reverses priority

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

describe the primary structure of proteins (2)

A

involves a sequence of amino acids linked together by peptide (amide) bonds) to form a polypeptide chain

listed in order from N-terminus to C-terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

describe connections of N and C termini in amino acid linkages (2)

A

N-terminus has an amine group, and C-terminus has a carboxylate group

N-terminus connects to the C-terminus of another amino acid, forming amide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

describe secondary structures of proteins (3)

A

areas of regular, local order in the protein backbone chain

tend to hold one of the four main types of structures (due to rotating restrictions)

chemical interactions between side chains can influence the shape of secondary structure

originate from conformations available due to amide bonds, and stereogenic enters which restrict rotations

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what are the four types of secondary structures

A

a-helix
b-sheet
loop
turn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

what 3 factors lead to the formation of a secondary structure

A

conformational restrictions in amide bonds

conformational restrictions between amide and alpha carbon

interactions between amide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

what two possible shapes can an amide form?

A

sigma cis (s-cis) or sigma trans (s-trans) conformations

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

describe the s-trans conformation of amides

A

2 large groups are far away and don’t interact

preferred/more stable conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
describe the s-cis conformation of amide
2 large groups eclipse and therefore interact not preferred/less stable
26
describe side chain interactions that occur in secondary structures of proteins + their result (4)
negative charges attract positive charges H bonding occurs between side chains and backbones of proteins non-polar side chains interact with other non-polar chains result = localized structure
27
what is a localized structure in terms of the secondary structure of proteins
the sum of all the effects of side chain interactions adding together to form a secondary structure formation
28
describe the alpha helix secondary structure of proteins (3)
corkscrew/spiral shape forms H bonds between amide groups about 4 amino acids apart represented by ribbon diagrams that follow plane of amide groups in backbone, and includes arrow pointing from N to C terminus
29
describe the beta structure of secondary proteins (overall)
can take shape of beta strand, beta sheet, or beta barrel
30
describe the structure of a beta strand (4)
a linear strand of amino acids zig-zag formation (because amides prefer s-trans formation) backbone organizes itself so everything is on same plane (so coplanar/flat in nature) side chains stick out on either side
31
describe the structure of a beta sheet (4)
formed by several beta strands associating together can be parallel or antiparallel held together by hydrogen bonds flat structures
32
describe the structure of a beta-barrel
beta sheets curling around themselves to form a cylinder formation
33
describe structure of a loop (2)
area with no defined secondary structure thin tube structures
34
describe structure of turns (3)
areas that change almost 180 degrees with length of 3-4 amino acids done because of H bonding between nearby amide groups peptide essentially kinds over onto itself and changes direction
35
describe tertiary structure of a protein (5)
overall 3D shape of protein combination of secondary structures added together result of interactions between non-adjacent regions mostly non-bonding interactions disulphide bonds primarily control structure (between 2 cysteine side chains)
36
what four attractractiv forces are involved in tertiary structures?
disulphide bonding ionic bonding hydrogen bonding van der waal interactions
37
what is disulphide bonding
most common/strongest covalent bond involves formation of disulphide bond (typically between 2 cysteine side chains)
38
what is ionic bonding
also known as salt bridge involves complete positive and complete negative charges being attracted to each other
39
what is hydrogen bonding?
involves hydrogen being attracted to a pair of electrons on an atom nearby
40
what are van der waal interactions
involve greasy side chains interacting with greasy side chains (non-polar non polar interactions) weak, but not important
41
what are van der waal interactions
non-polar non-polar interactions (greasy side chains interacting with greasy side chains) weakest, but most important interaction
42
why are van der waal interactions important for tertiary structures (4)
allow for side chains on inside of protein to be non-polar, creating an inner non-polar environment side chains on outside are polar, creating polar environment non bonding interactions (H bonding and dipole) are weaker on the outside because polar + polar = weakened bonds. nonbonding interactions are stronger on inside because polar + non polar = stronger bonds. strong inner bonds are what hold the protein together
43
what are quaternary structures
occurs when two or more tertiary structures of proteins come together to generate larger protein
44
what type of interactions occur in quaternary structures? why so strong? (4)
protein protein interactions strong because: -lots of surface area -lots of chemical interactions -exclusion of water from space between so proteins stick tightly together
45
is most of a protein active or scaffold?
most of protein is just scaffold, only a small part is active
46
what are the four types of protein targets for drugs?
enzymes receptors ion channels structural proteins
47
what does a drug do if an enzyme is its target in general?
stops enzyme from working (inhibitors)
48
what does a drug do if it has receptor for target?
activates (agonist) or deactivates (antagonist)
49
what does a drug do if it has ion channel for target
opens or closes the channel
50
what does drug do if it has structural protein for target?
interferes with assembly/disassembly of protein structures
51
how do enzymes catalyze reactions?
creates a custom environment for transition state of reaction bind to transition states and lower transition state energy/activation energy accelerating the reaction
52
describe general process of enzyme catalyzed reactions? (3)
enzyme binds to substrate resulting in some sort of shape change and forming enzyme-substrate complex reaction occurs forming the enzyme-product complex product is formed and separates from enzyme
53
what are the two main theories of enzymatic conformational change? which is correct?
lock and key - enzyme is perfect shape to fit into substrate induced fit - enzyme/substrate binding changes shape both correct, but induced fit more realistic
54
what are Michaelis Menten kinetics?
used to describe efficiency of enzyme shows kinetics behind enzyme catalyzed reactions
55
what does a Michaelis Menten plot do?
tracks how an enzyme produces product over time
56
what are the 4 main types of enzyme inhibition?
competitive inhibition non-competitive inhibition un-competitive inhibition irreversible inhibition
57
describe competitive inhibition (30
drug competes with substrate molecule for the active site binds to active site and changes its shape prevents substrate from binding, therefore product cannot be produced
58
describe kinetics of competitive inhibition (3)
alters Km and Kcat, but Vmax stays same Y-intercept stays same Slope changes
59
what type of inhibitor is disulfiram? what does it do?
drug for alcoholics inhibits/blocks acetaldehyde dehydrogenase (chemical that stops body from getting sick due to hangover) essentially produces wicked hangover to prevent alcoholics from drinking
60
describe non-competitive inhibition (3)
inhibitor binds to enzyme in spot other than the active site causes a conformational change to occur which prevents the substrate from being able to properly bind to active site prevents formation of the enzyme substrate complex
61
describe kinetics of non-competitive inhibition
changes both slope and y-intercept alters Kcat and Vmax, but does not change Km
62
describe uncompetitive inhibition (3)
very rare inhibitor binds to enzyme-substrate complex instead of enzyme itself (so attaches after substrate has already binded to enzyme) destroys the catalytic ability of it ES complex (catalysis cannot occur)
63
describe kinetics of uncompetitive inhibition
alters Kcat Km and Vmax
64
describe irreversible inhibitors
covalent (suicide) inhibitors bond covalently to enzyme (usually in active site) and alter conformation/disable functional groups
65
what is a receptor
a molecule that moves information from one side of membrane to other specialized proteins in cell membrane
66
how do receptors transfer information across membrane (4)
messenger approches receptor shape of receptor changes upon interaction receptor on other side of membrane becomes activates/changes shape allowing info to be carried once information has been transmitted, receptor spits out messenger and process starts again
67
what two ways does information transfer in receptors take place?
binding of messenger changing conformation of receptor allowing another molecule to bind or be released binding of messenger changing conformation of receptor creating an enzyme active site on receptor
68
how do ion channels work
acts like a valve when messenger binds, valve opens allowing ions to flow from one side of membrane to other
69
what are the 5 main classes of drugs
agonists antagonists allosteric antagonists partial agonists inverse agonists
70
what are agonists (3)
activates the receptor in a normal way (essentially acts as messenger) usually binds in same place as messenger, and induces shape change very similar to normal messenger biological response increases with increased concentration
71
what is an allosteric modulator? what drug class does it correspond with? (4)
type of agonist binds to receptor, but not in same place as normal messenger alters shape/sensitivity of receptor towards normal messenger which alters the way the two interact going forward work with ion channels
72
what are antagonists (4)
binding induces abnormal shape change that results in no signal transmission changes shape of receptor into shape that is not accessible by regular messenger molecule so that is cannot bind and info cannot be transmitted may bind at same site as messenger or different essentially prevent transmission of information
73
what are allosteric antagonists (3)
binds to active site or somewhere near does not bind at same place as messenger disrupts shape of receptor so that messenger cannot bind and therefore information cannot be transmitted
74
what are partial agonists
similar to agonists but not as strong binds to receptor and produces non-ideal conformational change.

Biopharmaceuticals Final (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions