W - BIOL200 - 2.1 PROTEINS

0.0(0)
studied byStudied by 0 people
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
Card Sorting

1/33

encourage image

There's no tags or description

Looks like no tags are added yet.

Study Analytics
Name
Mastery
Learn
Test
Matching
Spaced

No study sessions yet.

34 Terms

1
New cards

What are the monomers of proteins?

Amino acids.

2
New cards

What are the 3 parts of an amino acid?

Amino group, carboxyl group, R group.

3
New cards

How many R groups exist?

20 different R groups.

4
New cards

What do R group interactions determine?

The 3D structure of proteins.

5
New cards

What are the types of R group properties?

Hydrophobic, positively charged, negatively charged, or special cases.

6
New cards

Name 3 amino acids with positive side chains.

Arginine, Histidine, Lysine.


7
New cards

Name 2 amino acids with negative side chains.

Aspartic acid, Glutamic acid.

8
New cards

Name 4 polar uncharged amino acids.

Serine, Threonine, Asparagine, Glutamine.

9
New cards

Name 4 hydrophobic amino acids.

Alanine, Valine, Leucine, Isoleucine.

10
New cards

Name 2 special case amino acids.

Proline, Glycine.

11
New cards

How are amino acids linked together?

By dehydration (condensation) reactions.

12
New cards

What bond is formed between amino acids?

Peptide bond.

13
New cards

Which groups form a peptide bond?

Carboxyl group of one amino acid and amino group of another.

14
New cards

What is the repeating backbone in a protein?

N–C–C.

15
New cards

What is the N-terminus of a protein?

The end with the amino group.


16
New cards

What is the C-terminus of a protein?

The end with the carboxyl group.

17
New cards

What is primary protein structure?

Sequence of amino acids.

18
New cards

What is secondary protein structure?

Hydrogen bonds forming alpha-helices or beta-sheets.

19
New cards

What is tertiary structure?

Interactions between R groups.

20
New cards

What is quaternary structure?

Interactions between multiple folded proteins.


21
New cards

What do enzymes do?

Speed up reactions (e.g., lactase breaks down lactose).

22
New cards

What is the transport function of proteins?

Move things across membranes (e.g., ion channels).

23
New cards

What is the support function?

Maintain structure (e.g., cytoskeleton).

24
New cards

What do signaling proteins do?

Communicate (e.g., insulin).

25
New cards

How do proteins help movement?

Move cells or parts of cells (e.g., cilia).

26
New cards

What is the defense function?

Immune protection (e.g., antibodies).


27
New cards

What determines protein folding shape?

Amino acid sequence and side group interactions.

28
New cards

What helps fold proteins properly?

Chaperones.

29
New cards

What happens when proteins lose their shape?

They become denatured.

30
New cards

Does the amino acid sequence change during denaturation?

No.


31
New cards

What bonds are found in protein structures?

  • Primary: covalent (peptide) bonds

  • Secondary: hydrogen bonds

  • Tertiary: hydrogen, disulfide, ionic, Van der Waals

  • Quaternary: same as tertiary

32
New cards

What are the building blocks of proteins?

An R group, a carboxyl group, and an amino group.


33
New cards

A beta sheet is an example of?

Protein secondary structure.

34
New cards

What affects protein 3D folding?

pH, temperature, and amino acid side chain properties.