3.2 Flashcards

(22 cards)

1
Q

What are R-groups?

A

Grouping of the 20 amino acids

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

What are proteins/polypeptides?

A

Amino acids joined by peptide bonds giving backbone

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

What is at the end of an amino acid sequence?

A

Carboxyl end (C-terminus) and amino end (N-terminu)

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

Describe protein structure

A

There are four levels
Different types of interactions holding 3D shape
Structure is necessary for function

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

How are amino acids linked?

A

By covalent bonds called peptide bonds

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

What is the primary structure of a protein?

A

The sequence of amino acids, determined by genetic info

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

What are the four levels of protein structure?

A

Primary, secondary, tertiary and quaternary

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

What makes up the secondary structure of proteins?

A

Coils and folds in the polypeptide chain
Coils are from hydrogen bonds between the polypeptide backbone
Typical structure include alpha helix and beta pleated sheet.

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

What makes up the tertiary structure of proteins?

A

Interactions between various R groups
Include hydrogen and ionic bonds and hydrophobic interactions
Strong covalent bonds called disulfide bridges may reinforce structure.

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

What makes a quaternary structure protein?

A

When a protein consists of multiple polypeptide chains

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

What physical and chemical conditions can affect structure of proteins?

A

pH, salt concentration, temperature

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

What was the process of Anfinsens experiment?

A

Used urea to disrupt hydrogen bonds and dneature ribonuclease A, unfolding into a linear non functional form.
When the denaturing agent was removed the protein resolved spontaneously to its natural function structure

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

What did Anfinsens experiment show?

A

The primary structure alone determines the secondary and tertiary structure of proteins

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

Describe spontaneous processes?

A

Can happen quickly or slowly
Enzymes increase the speed
Free-energy change is negative
Energy is released = exergonic reaction

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

Describe non-spontaneous reactions

A

Will only occur if energy is provided
Free-energy change is positive
Energy is required = endergoinc reaction

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

What ar the three main kinds of work in a cell?

A

Chemical work: push in ednergoinc reactions
Transport work: pumping substances against the direction of spontaneous movement
Mechanical work: such as contraction of muscles

17
Q

What is ATP composed of?

A

Ribose, adenine and three phosphate groups

18
Q

How is energy released from ATP?

A

The bonds between the phosphate groups can be broken in hydrolysis, this releases energy

19
Q

What is a catalyst?

A

A chemical agent that speeds up a reaction without being consumed

20
Q

How do enzymes speed up reaction?

A

They lower the activation energy,
They do not affect the change in free energy

21
Q

What are competitive inhibitors?

A

Bind to the active site of an enzyme competing with the substrate

22
Q

What are non-competitive inhibitors?

A

Bind to another part of an enzyme causing the enzyme to change shape making the active site less effective.