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Biology > Functional Groups and Bio Intro > Flashcards

Functional Groups and Bio Intro Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Polar

A

Have a charge, dissolves in water

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2
Q

Polar Functional Groups

A

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

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3
Q

What is an Acid

A

Proton Donor

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4
Q

Polar Functional groups in amino acids

A

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

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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.

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6
Q

Sulfhydryl group purpose

A

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

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7
Q

Purpose of ATP

A

Energy source for muscle contraction

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8
Q

Guanosine Triphosphate purpose

A

Energy source for Protein synthesis

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9
Q

Non-polar functional group

A

CH3, hydrophobic

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10
Q

Macromolecules

A

large organic polymers formed from monomers

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11
Q

4 classes of macromolecules

A

proteins, lipids, nucleic acids, and carbohydrates

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12
Q

Catabolism

A

Breaking down macromolecules to release energy. Opposite of Anabolism

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13
Q

Which cells in the body use proteins?

A

All of them.

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14
Q

Polypeptides

A

Polymer of amino acids linked by peptide bonds.

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15
Q

Structure of proteins

A

Consists of one or more polypeptide chains

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16
Q

7 functions of proteins

A

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

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17
Q

Collagen

A

Protein for structural support. Present in animal connective tissue.

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18
Q

Na, K-ATPase

A

Transport protein that transports NaK across the membrane

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19
Q

Hemoglobin

A

Protein that transports oxygen

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20
Q

Insulin

A

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

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21
Q

Receptor Protein

A

Detect chemical signals released by other cells

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22
Q

Actin and Myosin

A

Proteins for muscle movement

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23
Q

Defensive Proteins

A

Antibodies

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24
Q

Enzymes

A

Substance that accelerates chemical reactions (biological catalyst)

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25
Q

How many different amino acids are used for protein synthesis in biological systems?

A

20

26
Q

Zwitterion

A

dipolar ion

27
Q

3 ionic states of amino acids

A

in acids - acts as base, one additional charge
In base - acts as acid, one less charge
Neutral - Zwitterion - neutral ion
Differentiating amino acids

28
Q

How to differentiate amino acids

A

look at R group (side chain)

29
Q

Alpha carbon

A

Central carbon of amino acid

30
Q

How many hydrophobic amino acids?

A

9 - derivatives of CH3 - nonpolar

31
Q

How many charged hyrdophilic amino acids

A

5

32
Q

Two types of hydrophilic amino acids

A

charged, uncharged

33
Q

How do you draw amino acids and polypeptides

A

From n-terminus (amino end) to C-terminus (carboxyl end) -left to right

34
Q

How long are polypeptides

A

A few amino acids in length to thousands

35
Q

Isoelectric point

A

pH at which a molecule has no net charge

36
Q

How many different polypeptides

A

Each polypeptide has a unique linear sequence of amino acids and isoelectric point

37
Q

What determines the isoelectric point of a polypeptide

A

R-chain

38
Q

What determines the primary protein structure

A

DNA sequence

39
Q

Two models for protein structure

A

Ribbon model and space filling model

40
Q

Secondary Structure

A

Visual, repeating structure -amino acids close together, backbone interactions

41
Q

Two types of secondary structure

A

Alpha helix and beta pleated sheet

42
Q

Amino acid residues

A

Individual amino acid after they link up with others to form polypeptide

43
Q

Alpha helix shape reason

A

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
Q

How are beta strands depicted

A

As flat arrows pointing towards the Carboxyl end (c-terminus)

45
Q

What keeps beta pleated sheets together

A

Hydrogen bonds

46
Q

Distance between H bonds of beta pleated sheets

A

No exact distance, unlike Alpha helix

47
Q

What reinforces the two types of secondary structures?

A

H bonds between the CO and NH groups of the polypeptide backbone.

48
Q

Phospholipid bilateral structure

A

Hydrophilic heads and hydrophobic tails.

49
Q

Only amino acid with SH

A

Cysteine

50
Q

Types of bonds which contribute to tertiary structure

A

Disulfide bridges, H bonds between charged Sid chains
Ionic bonds between charged side chains (salt bridge)
Hydrophobic interactions between non polar side chains.

51
Q

How is a salt bridge formed?

A

Positive and negative r groups fold onto each other and form a salt bridge (ionic bridge)

52
Q

Hydrophobic side chain interaction

A

Non polar side chains fold onto each other to escape aqueous environment.

53
Q

How strong are disulfide bridges?

A

Very strong - a type of covalent linkage

54
Q

How do you break salt bridges?

A

Add salt

55
Q

How do you break disulfide bridges?

A

Increase temperature significantly

56
Q

When is a quaternary structure visible?

A

When a protein is made of more than one polypeptide

57
Q

Which forces hold together the quaternary structure?

A

Same as tertiary (covalent, weak)

58
Q

Quaternary structure of collagen

A

3 helical polypeptides supercoiled into a triple helix

59
Q

Quaternary structure of Hemoglobulin

A

Globular protein composed of 4 polypeptides

60
Q

Number of polypeptides that make up Na, K-ATPase

A

2-3

Biology (5 decks)

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