Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Chem 1110 > Chapter 10: Proteins, Amino Acids, Enzymes, Peptides > Flashcards

Chapter 10: Proteins, Amino Acids, Enzymes, Peptides Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

What are the 10 essential amino acids

A

Arginine
Histidine
Isoleucine

Leucine
Lysine
Methionine

Phenylalanine
Threonine
Tryptophan
Valine

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

What are the 10 non essential amino acids

A

Alanine
Asparagine
Aspartate

Cysteine
Glutamate
Glutamine

Glycine
Proline
Serine
Tyrosine

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

What are essential amino acids?

A

Essential amino acids cannot be made by the body. (must get from food)

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

What are non essential amino acids

A

our bodies can produce the amino acid, even if we do not get it from the food we eat.

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

what is an amino acid structure?

A

central carbon atom with -COOH,-H2N, and a R group
So
H
|
H2N—C—COOH
|
R group

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

What is the acid base nature of amino acids

A

Amino acids can function as both Bronsted-Lowry acids and bases because they have both acidic and basic functional groups

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

What is a Bronsted-Lowry acid?

A

any species that can donate a proton

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

What is a Bronsted-Lowry base?

A

Anything that can accept a proton

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

What is the isoelectric point?

A

is the pH at which a molecule has a net charge of zero

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

How do you find the net charge?

A

Subtract protons and electrons

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

How do you know the atomic number?

A

The number of protons

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

What is the mass number?

A

Protons+neutrons

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

The zwitterion of an amino acid exists at a pH _____ to the isoelectric point

A

The zwitterion of an amino acid exists at a pH equal to the isoelectric point

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

Amide bond condensation reaction is when

A

The −OH from the carboxyl group of one amino acid combines with a hydrogen atom from the amine group of the other amino acid to produce water

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

what is an example of an Amide bond condensation reaction

A

when ethanol is heated in the presence of sulfuric acid, diethyl ether and water are formed:

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

What is the N terminus?

A

H2N-CH-C
the first part of the protein that exits the ribosome during protein biosynthesis

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

What is the C terminus

A

C-OH
the end of an amino acid chain

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

what are the 4 levels of the 3D structure of proteins

A

primary, secondary, tertiary, and quaternary structure.

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

What is the primary structure of proteins

A

sequence of a chain of amino acids (Looks like a long snake)

20
Q

What is the secondary structure of proteins

A

hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern. (Looks like folded paper)

21
Q

What is the tertiary structure of proteins

A

Three dimensional folding pattern of a protein due to side chain interactions (looks like the snake is laying onto of itself)

22
Q

What is the quaternary structure of proteins

A

Protein consisting of more Than one amino acid chain (Two snakes laying on top of each other)

23
Q

what causes a protein to denature

A

Heat

24
Q

what causes a protein to renature

A

when the denaturing influence is removed

25
Q

What is a receptor? What’s its function?

A

-a protein molecule to which substances like hormones, drugs, and antigens can bind.
-This allows them to change the activity of a cell

26
Q

What is transporters? What is its function?

A

-Transporters (membrane transport/carrier proteins) are specialized membrane-spanning proteins
- Assist in the movement of ions, peptides, small molecules, lipids and macromolecules across a biological membrane.

27
Q

What is the transportation of oxygen function

A

-fundamental to aerobic respiration and the survival of organisms through facilitated diffusion

28
Q

what is the antibody function? How do they work?

A

-protect you when an unwanted substance enters your body
-Antibodies bind to these unwanted substances in order to eliminate them from your system.

29
Q

What are enzymes function?

A

help speed up metabolism, or the chemical reactions in our bodies.

30
Q

What is the active site of an ezyme

A

The part of the enzyme where the substrate binds

31
Q

What is the substrate of an enzyme

A

a molecule that an enzyme reacts with at the active site

32
Q

What is the enzyme substrate complex of an enzyme?

A

an enzyme with its substrate attached at the enzyme’s active site

33
Q

What is substrate specificityof an enzyme

A

The preference of an enzyme for one specific substrate (not all enzyme active sites will accept a substrate)

34
Q

What are The two ES models of enzymes?

A

-The lock and key model: substrate is the key enzyme is the lock
-The induced fit model: enzyme active site changes as well as the substrate to fit

35
Q

How does proximity change enzyme reaction rate

A

Enzyme proximity effect means the increasing of reaction rate by causing a higher probability of collision when reactants are closer together

36
Q

How does orientation of a substratechange enzyme reaction ?

A

-the enzyme constrains the substrates into specific reactive conformations,
- increases the probability that reactants will collide in the correct orientation to react

37
Q

How does substrate concentration change enzyme reaction rate

A

At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration

38
Q

How does pH change enzyme reaction rate

A

Changing the pH outside of this range will slow enzyme activity

39
Q

How does inhibitors change enzyme reaction rate

A

fewer substrate molecules can bind to the enzymes so the reaction rate is decreased.

40
Q

What are the 3 types of enzyme inhibitors

A

-Competitive Inhibition: binds to the active site and prevents the substrate from binding there.
-Non-competitive Inhibition: binds to a different site on the enzyme; it doesn’t block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.
-Uncompetitive Inhibition: when an inhibitor binds to an allosteric site of a enzyme, but only when the substrate is already bound to the active site.

41
Q

The structure of glycine

A

……………………………..H
|
HO2CCH2NH2 (H2N-C-COOH)
|
H

42
Q

The structure of alanine

A

………H
|
(NH2-C-COOH)
|
CH3

43
Q

The structure of serine

A

COOH
|
H2N-C-H
|
CH2OH

44
Q

The structure of lysine

A

COOH
|
H2N-C-H
|
CH2
|
CH2
|
CH2
|
CH2
|
NH2

45
Q

The structure of aspartic acid

A

COOH
|
H2N-C-H
|
CH2
|
COOH

Chem 1110 (9 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions