Brainscape's Knowledge GenomeTM

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


See full index

Miller OnRamps Biology > Amino Acids & Proteins > Flashcards

Amino Acids & Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Structure of proteins influences…

A

The binding of different molecules

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

All peptides, polypeptides and proteins in the mammals are polymers of…

A

Alpha-L-amino acids

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

How many alpha-amino acids are used to make up proteins

A

20

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

Give the general structure of an amino acid

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

Which functional groups are found on alpha-amino acids, peptides and proteins?

A
  • Carboxylic (-COOH)
  • Amino (-NH2)

Attached to the same carbon atom (alpha carbon)

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

All amino acids in proteins exhibit which configuration?

Why?

A

Absolute steric configuration

Based on: Proteinogenic L-amino acids, related to L-glyceraldehyde

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

What is a monoamino monocarboxylic acid?

A

Amino acids with aliphatic R-groups

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

List the monoamino monocarboxylic acids

A
  • Glycine
  • Alanine
  • Valine
  • Leucine
  • Isoleucine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

List the non-aromatic amino acids with Hydroxyl R-groups

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

List the amino acids with sulphur-containing R-groups

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

Give the amino acids with aromatic rings

A
  • Phenylalanine
  • Tyrosine
  • Tryptophan
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Give the interaction

A

Hydrogen bond

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

Name the interaction

A

Van der Waals

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

Name the interaction

A

Disulphide bridge

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

Give the interaction

A

Ionic bond

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

What is happening in the figure?

A
  • Condensation of two amino acids
  • Forming a dipeptide with a peptide bond
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is shown?

What is shown in the red and blue circles?

A

Polypeptide chain

  • Red circle: N-terminal
  • Blue circle: C-terminal
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Isoelectric point

A

pH value where the amino acid has no net charge

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

What classifies globular proteins?

A

They are water soluble

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

What classifies fibrous proteins?

A

They are water insoluble

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

What are intermediate proteins?

A
  • Water soluble
  • Rod-like
  • Found in myosin and fibrinogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

List the protein classifications differing by shape or water solubility

A
  • Globular proteins
  • Fibrous proteins
  • Intermediate proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

List the proteins classifications by differing compositions

A
  • Simple proteins
  • Conjugated proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Simple proteins

A

During hydrolysis: Only amino acids/amino acid derivatives produced

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

Conjugated proteins

A

Conjoined simple protein and non-protein compound

26
Q

Prosthetic group of: Glycoproteins

A

Carbohydrates

27
Q

Prosthetic group of: Nucleoproteins

A

Nucleic acids

28
Q

Prosthetic group of: Phosphoproteins

A

Phosphoric acid

29
Q

Prosthetic group of: Chromoproteins

A

Coloured prosthetic group

30
Q

Example of a hemoprotein

A

Haemoglobin

31
Q

Lipoproteins contain…

A

Lipid molecules

32
Q

Prosthetic group of: Flavoproteins

A

Flavin

33
Q

Prosthetic group of: Metalloproteins

A

Metals

34
Q

List 3 conjugated protein types

A
  • Glycoproteins
  • Nucleoproteins
  • Phosphoproteins
35
Q

List protein types differing by function

A
  • Contractile proteins
  • Transport proteins
  • Enzymes
  • Protein hormones
  • Toxic proteins
36
Q

Primary structure of proteins

A

Amino acid sequence

37
Q

Secondary structure of proteins

A
  • α-helix/Beta-pleated sheet/Collagen helix
  • Regularly repeating units
38
Q

Tertiary structure of proteins

A
  • Polypeptide chain
  • 3-D structure by complete folding
39
Q

Quarternary structure of proteins

A

Assembled subunits

40
Q

In moist heat:

Alpha-keratin →

A

Beta-keratin

41
Q

Native conformation

A
  • The 3-D conformation of a protein
  • Stable and active at optimal temp. and pH
42
Q

Function of proteins arises from…

A

Chain-conformation

(Secondary & Tertiary structure)

43
Q

Functional shape of a protein occurs during which stage?

A

Protein folding

(Active, native conformation formation)

44
Q

Denaturation of proteins

A

Unfolding of chains

(Can be reversible - renaturation)

45
Q

How does heat denature proteins?

Examples

A

Breaks:

  • Hydrophobic interactions
  • Hydrogen bonds

Examples:

  • Egg when it is fried
  • Skin when it is burned
46
Q

How do acids and bases denature proteins?

A

By breaking ionic bonds

47
Q

How do reducing/oxidising agents denature proteins?

A

Convert:

Disulphide bonds → free sulfhydryl groups

48
Q

How do hydrogen-bonding solvents denature proteins?

Example

A

Disruption of hydrogen bonds

Ethanol - precipitates bacteria proteins

49
Q

How do heavy metal ions denature proteins?

Example

A

React with sulfhydryl bonds to form carboxylate ions

AgNO3 previously used to treat eyes of newborns for gonorrhoea

50
Q

How does salting-out denature proteins?

Example of use

A

Removes the hydrate hull

Used in the separation of proteins

51
Q

Denaturing agents used in gel electrophoresis

A
  • Sodium dodecyl sulphate
  • Mercaptoethanol
52
Q
A

Haemoglobin - Quarternary structure

53
Q

Peptide bond:

  • Bond type
  • Location
A
  • Primary, covalent bond
  • Between amino acids
54
Q

Disulphide bond:

  • Bond type
  • Location
  • Example
A
  • Primary, covalent bond
  • Between -SH containing side chains
  • 2 x Cysteine molecules form these bonds → Cystine formed
55
Q

Ionic bond:

  • Bond type
  • Location
A
  • Primary bond
  • Between polar, charged side chains
  • Between carboxyl group of an acidic and a basic amino group
56
Q

Dipol-dipol interaction:

  • Bond type
  • Location
A
  • Secondary bond
  • Between polar, non-charged sidechains

The partially negative portion of molecule attracted to partially positive portion of the other

57
Q

Van der Waals dispersion force:

  • Bond type
  • Location
A
  • Secondary, hydrophobic bond
  • Between non-polar side chains
  • Weakest of all intermolecular forces*
  • Used when numerous atoms are present*
  • A temporary* partial negative charge on atoms
58
Q

List the bonds of the secondary and tertiary structures

A
  • Disulphide bond
  • Ionic bond
  • Dipol-dipol interaction
  • Van der Waals dispersion force
  • H-bonds
59
Q

List the bonds of the quarternary structure

A
  • Dispersion
  • Dipol
  • H-bond
  • Disulphide bond
60
Q

Give examples of acidic amino acids

A
  • Glu
  • Asp
61
Q

Give examples of basic amino acids

A
  • Lys
  • Arg
  • His

Miller OnRamps Biology (8 decks)

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