Brainscape's Knowledge GenomeTM

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


See full index

Chemistry > Proteins > Flashcards

Proteins Flashcards

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

What makes a protein?

A

Amino acid

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

What amino group does protein have?

A

Nitrogen and hydrogen

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

Type of acid group protein has?

A

Carboxylic acid

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

Where does the substituent R belong?

A

Alpha carbon

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

What is the only form active in biological systems?

A

L-amino acids

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

What amino acid does not have a stereoisomer?

A

Glycine

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

Why does glycine not have a stereoisomer?

A

The functional group on glycine is a hydrogen making it a CH2 (not a chiral).

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

What happens in a Thiol?

A

Has a sulfur and hydrogen.

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

What happens in a alcohol?

A

Oxygen and hydrogen

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

What type of amino acid is Cystine?

A

Polar amino acid

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

What type of amino acid is Glycine?

A

Non polar amino acid

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

What describes cystine?

A

Sulfhydryl and thiol

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

Nonpolar amino acids have what type of intermolecular forces?

A

Dispersion force

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

What amino acid can act as a buffer?

A

Basic and acidic amino acids.

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

What amino acids form ions?

A

Basic and Acidic amino acids.

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

What is a zwitterion?

A

Ion carrying both a positive and negative charge .

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

Reason for zwitterions?

A

Non ionized form doesn’t exist.

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

What happens with Cysteine?

A

It can oxidize and produce disulfide linkage

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

What is a disulfide linkage in Cysteine?

A

When 2 cysteine make a covalent bond.

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

To make a polypeptide backbone/protein, what chemical property has to occur?

A

Condensation

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

How many amino acid residues in insulin?

A

51

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

What happens when the amino acid residues connect in insulin?

A

It is no longer an amino acid

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

It is only an amino acid when it is ___?

A

Free floating

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

What is the opposite of condensation?

A

Hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

How to get amino acid back out?

A

Hydrolyze the protein.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Hydrolysis occurs under acidic or basic conditions?

A

Acidic conditions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What happens when we eat protein?

A

Stomach acid hydrolyzes it (breaks it down)

28
Q

How do you disrupt a primary structure?

A

Hydrolysis

29
Q

What structure are A-helix and B-sheet?

A

Secondary structures

30
Q

As a secondary structure,what are they governed by?

A

Hydrogen bonding

31
Q

What are primary structures?

A

List of amino acid residues

32
Q

What are tertiary structures?

A

Overall 3D shape

33
Q

What are quaternary structures?

A

Multiple subunits combining together to form a larger protein

34
Q

What is a peptide bond?

A

A bond that occurs when oxygen as polysaccharide or disaccharide has a glycocidic linkage.

35
Q

What is a peptide linkage?

A

An amide linkage only when talking abt peptides.

36
Q

What do amino acid residues specifically make?

A

Peptide linkages which are a type of amide.

37
Q

What can amide be made of?

A

Anything that has nitrogen or carboxylic acid.
When talking about amino acids = peptide linkages (formed)

38
Q

What is the peptide linkage name purpose? What is the reaction?

A

What brings them together and reaction is condensation reaction (water is produced, requires heat/enzyme)

39
Q

Is insulin a protein or polypeptide?

A

Polypeptide

40
Q

How many amino acid residues in a polypeptide?

A

50

41
Q

What is a fibrous classification?

A

Muscles, hair, etc..

42
Q

What is a globular classification?

A

Insulin, hemoglobin, etc.. (globs around)

43
Q

What is the size of proteins?

A

6000 to 10^6 amu

44
Q

Are proteins too large or small to pass through cell membranes?

A

Too large

45
Q

What happens when you end up with a lot of proteins in your blood?

A

Something bad happened to that cell to let proteins in blood.

46
Q

What behaves as buffers in proteins!

A

Isoelectric points

47
Q

What happens when changing the pH in proteins?

A

It can denature them

48
Q

What are isoelectric points?

A

The point of which the net overall charge of 0

49
Q

Functions of proteins?

A

Catalytic, structural, and storage, protective, regulatory, nerve impulse transmission, movement, and transport

50
Q

Catalytic function

A

Proteins acting as enzymes facilitating biochemical reactions w/ increased rates and specificity

51
Q

Structural function

A

All structure in body is protein. (Ex:collagen and keratin)

52
Q

Storage function

A

Proteins can store ions and molecules (ex: ferritin =storage of iron, ovalbumin=storage of amino acids in birds)

53
Q

Protective function

A

Proteins protect body from antibodies to clotting factors

54
Q

Regulatory functions

A

Proteins and peptides regulate processes in the form of hormones.

55
Q

Nerve impulse transmission function

A

Proteins act as receptors of neurotransmitters during synapsis (ex: vision process starts with protein)

56
Q

Movement function

A

Muscle contraction is coordinated by two proteins: actin and myosin

57
Q

Transport function

A

Nutrients like fatty acids, vitamins, minerals, oxygen are moved through body by proteins

58
Q

What is associated with the primary level?

A

Only has chemical properties associated

59
Q

How do you disrupt the primary level?

A

Glycolysis (break amino acids apart)

60
Q

How to make more amino acids to polypeptide

A

Condensation

61
Q

What affects the primary level?

A

Condensation and hydrolysis

62
Q

What holds the secondary level together?

A

Hydrogen bonding

63
Q

Tertiary level

A

All the potential intermolecular forces and chemical bonds.

64
Q

What holds the tertiary level?

A

All chemical and physical properties (disulfide linkages, covalent bond, salt bridges, ionic bonding, hydrogen bonding, hydrophobic/hydrophilic interactions)

65
Q

What is hydrolysis?

A

Strong acid or base breaks a peptide linkage resulting in smaller peptide or amino acids. Breakups the primary structure.

66
Q

Denaturation

A

Breaking secondary, tertiary, or quaternary folding into what it wants.

Chemistry (10 decks)

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