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Chemistry 1120 > Chapter 18 > Flashcards

Chapter 18 Flashcards

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1
Q

The pH at which a sample of amino acids has equal numbers positive and negative charges

A

Isoelectric point

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2
Q

What does an amino acids isoelectric point influence?

A

Protein solubility and determines which amino acid in enzymes participate in enzyme reactions

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3
Q

Amino acids that can form crystals, have high melting points, are soluble in water but not hydrocarbon solvents are what?

A

Pure amino acids

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4
Q

Amino acids that accept proteins of their basic COO- group to leave only a positively charged NH3+ are what?

A

Low pH amino acids

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5
Q

Amino acids that lose protons from their acidic NH3+ group to leave only negatively charged COO- groups are what?

A

High pH amino acids

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6
Q

How many amino acids are chiral? Which ones aren’t?

A

19 are chiral, glycine isn’t (it’s identical)

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7
Q

Do right or left handed enantiomers make proteins

A

Left handed enantiomers

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8
Q

The sequence in which amino acids are linked by peptide bonds in a protein

A

Primary structure

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9
Q

T or F

Primary structures form ridged planar peptide units

A

True

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10
Q

Regular and repeating structural patterns created by hydrogen binding between backbone atoms in neighboring segments of protein chains

A

Secondary structure

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11
Q

What are the two kinds of repeating patterns of secondary structures?

A

Alpha helix and beta sheets

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12
Q

Do alpha helixes and beta sheets hydrogen bond?

A

Yes to keep backbone in place

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13
Q

Overall 3- dimensional shape that results from the folding of a single protein chain

A

Tertiary structure

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14
Q

The way in which two or more protein chains aggregate to form large ordered structures

A

Quaternary structure

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15
Q

What are the two protein types of secondary structure?

A

Fibrous protein and globular protein

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16
Q

Tough insoluble protein whose protein chains form fibers/ sheets is globular or fibrous protein?

A

Fibrous

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17
Q

Water soluble protein whose chain is folded in compact shape with hydrophilic groups on outside is globular or fibrous protein?

A

Globular

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18
Q

Extremely stable structure where protein chain forms right handed coil stabilized by hydrogen bonds between peptide groups along its backbone

A

Alpha helix

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19
Q

Protein structure where adjacent protein chains in same/ different molecules are held together by hydrogen bonds along its backbone forming a flat sheet structure

A

Beta sheets

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20
Q

What protein is fibrous and makes up about 30% total proteins?

A

Collagen

21
Q

Protein hydrolysis is where peptides turn into _____

A

Amino acids

22
Q

Is an acidic or basic solution better for hydrolysis and why?

A

Acidic because a basic solution can destroy some amino acids

23
Q

What is a protein with the shape in which it exists naturally in living organisms? What type of protein structure is it?

A

Native structure, can be any 1-4 protein structures

24
Q

A disruption in the shape of the protein that does not affect the order of amino acids within a protein chain

A

Denaturation

25
Q

Which structures are and are not affected by denaturation

A

Only primary protein structures not lost
Other structures lost because of non covalent interactions or disulfide bonds leaving

26
Q

Denaturation can be caused by heat, ______, ________, organic compounds, ___, or _________.

A

Mechanical agitation
Detergents
Organic compounds
pH changes
Inorganic salts

27
Q

Can renaturation happen?

A

Possibly but not usually

28
Q

peptides and proteins are always written with the ___ terminal on the left and the ___ terminal on the right

A

N
C

29
Q

The C terminal amino acid has a free ____ group at the end of the protein

A

-COO group

30
Q

The N terminal amino acid has a free _____ group that’s at the end of the protein

A

-NH3+

31
Q

Individual amino acids joined in the polypeptide chain are called what?

A

Residues

32
Q

Why are proteins usually least soluble in water at their isoelectric point?

A

At isoelectric point their neutral which makes them least soluble (charged proteins are more soluble)

33
Q

What type of bonding is responsible for secondary structures?

A

Hydrogen bonding

34
Q

Is hydrogen bonding covalent or noncovalent?

A

Noncovalent

35
Q

Are alpha helixes usually fibrous or globular?

A

Fibrous (hair, nails, wool)

36
Q

Are B-sheets usually fibrous or globular?

A

Globular

37
Q

Spontaneous folding into correct tertiary structures is caused by _____ residues interacting with aqueous environments and _____ residues folding away and into each other

A

Hydrophilic
Hydrophobic

38
Q

What is a conjugated protein?

A

Protein with one or more non protein molecules

39
Q

Why is cysteine such an important amino acid for defining tertiary structure of some proteins?

A

Disulfide bonds stabilize tertiary structure

40
Q

Which structure coils and fold the entire protein chain?

A

Teritary

41
Q

Which structure orients segments of polypeptides into patterns?

A

Secondary

42
Q

What type of bonds hold amino acids together in primary structure?

A

Peptide bonds

43
Q

What is the minimum number of polypeptide chains necessary for quaternary structures to exist?

A

2

44
Q

Myoglobin is an example of a ____ protein

A

Conjugated

45
Q

Keratin and collagen are related to ____

A

Structure

46
Q

______ functions to carry oxygen in red blood cells

A

Hemoglobin

47
Q

What type of bonds connect insulin?

A

Disulfide bonds

48
Q

What is the difference between protein digestion and denaturation?

A

Digestion= protein —> amino acids
Denaturation= 4 protein —> 1 protein and loss of function

49
Q

Does protein hydrolysis end with the amino acids losing function?

A

No loss of function

Chemistry 1120 (16 decks)

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