Functional Groups and Bio Intro Flashcards

1
Q

Polar

A

Have a charge, dissolves in water

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

Polar Functional Groups

A

Hydroxyl, Carbonyl, Carboxyl, Amino (NH2), Sulfhydryl (SH), Phosphate (OPO32-)

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

What is an Acid

A

Proton Donor

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

Polar Functional groups in amino acids

A

Amino group and Carboxyl (acid), Sulfhydryl (SH)

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

Is an amino group an acid?

A

They can function as both acid and base. In amino acids, they function as a base.

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

Sulfhydryl group purpose

A

Involved in the folding of proteins. Has the ability to form disulfide bridges in proteins

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

Purpose of ATP

A

Energy source for muscle contraction

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

Guanosine Triphosphate purpose

A

Energy source for Protein synthesis

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

Non-polar functional group

A

CH3, hydrophobic

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

Macromolecules

A

large organic polymers formed from monomers

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

4 classes of macromolecules

A

proteins, lipids, nucleic acids, and carbohydrates

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

Catabolism

A

Breaking down macromolecules to release energy. Opposite of Anabolism

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

Which cells in the body use proteins?

A

All of them.

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

Polypeptides

A

Polymer of amino acids linked by peptide bonds.

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

Structure of proteins

A

Consists of one or more polypeptide chains

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

7 functions of proteins

A

Structural support, transport, hormonal, receptor, movement, defensive, enzymatic

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

Collagen

A

Protein for structural support. Present in animal connective tissue.

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

Na, K-ATPase

A

Transport protein that transports NaK across the membrane

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

Hemoglobin

A

Protein that transports oxygen

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

Insulin

A

Hormonal protein - first synthesized by Canadian (don’t have to know)

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

Receptor Protein

A

Detect chemical signals released by other cells

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

Actin and Myosin

A

Proteins for muscle movement

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

Defensive Proteins

A

Antibodies

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

Enzymes

A

Substance that accelerates chemical reactions (biological catalyst)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
How many different amino acids are used for protein synthesis in biological systems?
20
26
Zwitterion
dipolar ion
27
3 ionic states of amino acids
in acids - acts as base, one additional charge In base - acts as acid, one less charge Neutral - Zwitterion - neutral ion Differentiating amino acids
28
How to differentiate amino acids
look at R group (side chain)
29
Alpha carbon
Central carbon of amino acid
30
How many hydrophobic amino acids?
9 - derivatives of CH3 - nonpolar
31
How many charged hyrdophilic amino acids
5
32
Two types of hydrophilic amino acids
charged, uncharged
33
How do you draw amino acids and polypeptides
From n-terminus (amino end) to C-terminus (carboxyl end) -left to right
34
How long are polypeptides
A few amino acids in length to thousands
35
Isoelectric point
pH at which a molecule has no net charge
36
How many different polypeptides
Each polypeptide has a unique linear sequence of amino acids and isoelectric point
37
What determines the isoelectric point of a polypeptide
R-chain
38
What determines the primary protein structure
DNA sequence
39
Two models for protein structure
Ribbon model and space filling model
40
Secondary Structure
Visual, repeating structure -amino acids close together, backbone interactions
41
Two types of secondary structure
Alpha helix and beta pleated sheet
42
Amino acid residues
Individual amino acid after they link up with others to form polypeptide
43
Alpha helix shape reason
H bonds form between amino acid residues located 4 amino acid places apart. H bonds force helical structure, otherwise wouldn't be able to form.
44
How are beta strands depicted
As flat arrows pointing towards the Carboxyl end (c-terminus)
45
What keeps beta pleated sheets together
Hydrogen bonds
46
Distance between H bonds of beta pleated sheets
No exact distance, unlike Alpha helix
47
What reinforces the two types of secondary structures?
H bonds between the CO and NH groups of the polypeptide backbone.
48
Phospholipid bilateral structure
Hydrophilic heads and hydrophobic tails.
49
Only amino acid with SH
Cysteine
50
Types of bonds which contribute to tertiary structure
Disulfide bridges, H bonds between charged Sid chains Ionic bonds between charged side chains (salt bridge) Hydrophobic interactions between non polar side chains.
51
How is a salt bridge formed?
Positive and negative r groups fold onto each other and form a salt bridge (ionic bridge)
52
Hydrophobic side chain interaction
Non polar side chains fold onto each other to escape aqueous environment.
53
How strong are disulfide bridges?
Very strong - a type of covalent linkage
54
How do you break salt bridges?
Add salt
55
How do you break disulfide bridges?
Increase temperature significantly
56
When is a quaternary structure visible?
When a protein is made of more than one polypeptide
57
Which forces hold together the quaternary structure?
Same as tertiary (covalent, weak)
58
Quaternary structure of collagen
3 helical polypeptides supercoiled into a triple helix
59
Quaternary structure of Hemoglobulin
Globular protein composed of 4 polypeptides
60
Number of polypeptides that make up Na, K-ATPase
2-3