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Biology 12U > 1.5 Proteins & Nucleic acids > Flashcards

1.5 Proteins & Nucleic acids Flashcards

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1
Q

Protein definition

A

A large molecule that consists of many amino acid subunits that are joined together by peptide bonds folded into a specific 3D shape

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2
Q

Nucleic acid definition

A

A blueprint for proteins that are synthesized in cells; stores hereditary information

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3
Q

All proteins are _________ that are composed of amino acid ________.

A

polymers; monomers

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4
Q

Amino acid definition

A

A molecule that contains a carboxyl group and an amino group; serves as the monomer subunit of proteins

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5
Q

Attached to the central carbon atom (beside the amino acid) is a variable side group, called an ___ ______, which gives each amino acid its distinct _____________.

A

R group; characteristics

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6
Q

There are __ different amino acid side groups, or ___ _____, ranging from a single hydrogen atom to complex carbon chains or rings

A

20; R groups

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7
Q

The one exception to the 20 different amino acid groups is the amino acid ______, which has a ring structure that includes the ______ and central carbon atoms.

A

proline; nitrogen

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8
Q

Among the polar side groups in amino acids, some carry a positive or negative _______ and
others act as _____ or _____.

A

charge; acids; bases

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9
Q

Many of the amino acid side groups contain a _______ functional group, such as -NH2, -OH,
-COOH, or -SH, which may interact with atoms located elsewhere in the same protein or with molecules and ions located ______ the protein.

A

reactive; outside

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10
Q

With few exceptions, all proteins in living things are an assembly of various numbers and
_________ of 20 different amino acids.

A

combinations

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11
Q

___ of these amino acids are considered
essential for humans because they can only be obtained from our ____. The rest can
be synthesized by the _____.

A

8; diet; cells

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12
Q

________ proteins provide much of the supportive framework of the cells

A

Structural

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13
Q

Defensive proteins called _________, which are found in the human body, help to fight off ________.

A

antibodies; infections

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14
Q

Hormones and other messenger chemicals in the cell are ______ proteins.

A

signal

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15
Q

Special proteins called ________ are largely responsible for making almost every __________ reaction possible. They _______ up the rate of chemical reactions.

A

enzymes; biochemical; speed

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16
Q

Structural protein function and example

A

Framework support

e.g. hair, tendons, and ligaments

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17
Q

Defensive protein function and example

A

Infection fighters

e.g. antibodies

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18
Q

Signal protein function and example

A

Messenger

e.g. hormones

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19
Q

Carrier protein function and example

A

Transport of materials

e.g. hemoglobin

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20
Q

Recognition and receptor protein function and example

A

Cellular markers

e.g. major histocompatibility complex

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21
Q

Enzyme protein function and example

A

Catalyst

e.g. amylase

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22
Q

Motile protein function and example

A

Movement

e.g. actin and myosin

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23
Q

Peptide bond definition

A

A covalent bond that links many amino acids into chains of subunits that make proteins.

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24
Q

Peptide bonds are formed by a ________ _______ reaction between the -NH2 group of one amino acid and the -COOH group of a second amino acid

A

dehydration; synthesis

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25
Q

An amino acid chain always has an group
at one end, called the __________, and a -COOH group at the other end, called the ____________

A

N-terminal end; C-terminal end

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26
Q

In cells, amino acids are added only to the
_____ end of the growing peptide strand.

A

-COOH

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27
Q

Peptide definition

A

A chain of amino acid subunits that are connected by peptide bonds

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28
Q

Polypeptide definition

A

A peptide with more than 50 amino acids

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29
Q

Protein definition

A

A protein is one or more polypeptides that are folded into a precise 3D shape.

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30
Q

True or false:

A protein can function without folding.

A

False

Only after folding occurs is the protein able to function.

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31
Q

The primary structure of a protein is the unique _______ sequence of its amino acids in
each __________ chain

A

linear; polypeptide

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32
Q

Changing even a single amino acid
in the primary structure will _____ the overall structure of the protein to some degree.
A single change can alter or even destroy the __________ function of the protein.

A

alter; biological

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33
Q

The possible combinations of lengthy primary structures are virtually _________.

A

limitless

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34
Q

Most polypeptides have portions that repeatedly _____ or fold into patterns and contribute to the overall _____ of a protein.

A

coil; shape

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35
Q

This secondary structure is the result of __________ bonding between different parts of the same amino acid _________.

A

hydrogen; backbone

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36
Q

Two common secondary structures are the _____-pleated (or ß-pleated) sheet and the ______-helix (or a-helix)

A

beta; alpha

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37
Q

A B-pleated sheet forms by a side-by-side _________ of the amino acid chain. B-pleated sheets play an important role in the strength of ______.

A

alignment; silk

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38
Q

An a-helix is a delicate ____ that is held together by ________ bonds between every _____ amino acid.

A

coil; hydrogen; fourth

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39
Q

An a-helix is found in ____ proteins and _______________ proteins, and it provides the necessary _________ for their functions.

A

thin; transmembrane; structure

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40
Q

The secondary structure of a protein is the result of _________ between atoms in the _________.

A

interactions; backbone

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41
Q

The tertiary structure of a protein is the overall ___ _______ of a protein due to a range of interactions among the amino acid _________

A

3D shape; R groups

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42
Q

It is in the tertiary structure that the interactions of the R groups determine the 3D _____ of the __________ chain.

A

shape; polypeptide

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43
Q

Hydrophobic interactions definition

A

Hydrophobic interactions are the interaction of non-polar side groups that cluster together as a
result of other amino acid R groups interacting with water.

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44
Q

Disulfide bridge definition

A

A disulfide bridge is the bond that is formed when the -SH groups of two cysteine amino acids line up and react to form an S-S covalent bond.

This is a strong bond that holds 2 parts of the
polypeptide strand together, stabilizing its shape.

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45
Q

The tertiary structure is critical to
the ________ of proteins, especially _______.

A

functions; enzymes

46
Q

Extreme conditions (such as temperature and pH) can _______ a protein, causing _______

A

unfold; denaturation

47
Q

Denaturation definition

A

The loss of both the structure and function of a protein

48
Q

Many proteins are composed of ____ polypeptides that come together to form the final functional proteins. This quaternary structure, which forms _______, exists
in many proteins.

A

2+; subunits

49
Q

The same bonds and forces that fold _____ polypeptide chains into tertiary structures (including hydrogen bonds, polar and non-polar attractions and disulfide linkages) also hold the ______ polypeptide chains together.

A

single; multiple

50
Q

Besides properly folded polypeptide chains, many proteins require _________ components, called ________ groups, to function.

A

non-protein; prosthetic

51
Q

Prosthetic group example

A

One example is found in hemoglobin, the major protein that is involved in transport in vertebrates.

In hemoglobin, the 4 polypeptides don’t bind the oxygen (it’s bound to heme groups, surrounded and held by polypeptides)

Each polypeptide chain contains 1 heme ring, in which there is a single iron (Fe2+) ion.

Therefore, there are 4 heme groups per hemoglobin, and 4 are carried.

52
Q

Many enzymes require prosthetic groups that contain ______ ions in order to function.

For example, some enzymes that are involved the process of cellular respiration require ______ ions.

A

metal; Mg2+

53
Q

The _______ of a protein influences and enables its _________.

A

shape; function

54
Q

Give an example of how shape influences a protein’s function

A

For example, long linear proteins align to form the strong fibres of silk, collagen, and keratin. This long linear formation provides the strength.

Compact globular proteins, such as the hemo
globin protein, are good for transport. Their shape enables them to be carried efficiently through red blood cells and the body.

55
Q

Enzymes and antibodies have special _______ that _____ specific molecules, allowing these proteins to carry out their ________.

A

pockets; bind; function

56
Q

DNA

A

stores hereditary information responsible for inherited traits in all eukaryotes, prokaryotes and many viruses.

57
Q

RNA

A

-hereditary molecule of some viruses
-several different forms of RNA involved in
protein synthesis in all cells.

58
Q

All nucleic acids are ________ of units called ___________.

A

polymers; nucleotides

59
Q

Nucleotide definition

A

Building block of nucleic acids; consists of a 5- carbon sugar, a nitrogenous base, and one to three phosphate groups linked together by covalent bonds

60
Q

In a nucleotide, each nitrogenous base links covalently to a 5- carbon sugar, either ________ or ________.

The two sugars differ only in the chemical group that is bound to the 2’-carbon: deoxyribose has an ___, and ribose has an ____ group.

A

deoxyribose; ribose; -H; -OH

61
Q

What are the 2 types of nitrogenous bases?

A

Pyrimidines and purines

62
Q

Pyrimidines

A

-single organic rings
-high nitrogen content

uracil (U), thymine (T), and cytosine (C)

63
Q

Purines

A

-two-ringed organic structures
-high nitrogen content

adenine (A) and guanine (G)

64
Q

DNA and RNA consist of chains of nucleotides, called __________ chains, with one nucleotide linked to the next by a single bridging ________ group between the 5’- carbon of one sugar and the 3’-carbon of the next sugar in line.

This type of linkage is called a _________ bond.

A

polynucleotide; phosphate; phosphodiester

65
Q

Phosphodiester bond definition

A

A link formed between nucleotides by a
phosphate bridge

66
Q

The arrangement of the alternating sugar and phosphate groups forms the ________ of a ______ ____ chain.

A

backbone; nucleic acid

67
Q

In a ___ chain, each nucleotide contains _________, a phosphate group, and one of the four bases A, T, G, or C.

A

DNA; deoxyribose

68
Q

In an ___ chain, each nucleotide contains _______, a phosphate, and one ofthe four bases A, U, G, or C.

A

RNA; ribose

69
Q

DNA is a double-stranded molecule in which the two strands of DNA run _________
to each other.

This means that they are oriented in the ________ direction relative to the sugar-phosphate backbone.

A

antiparallel; opposite

70
Q

In a sugar phosphate backbone, the end with the phosphate group is referred to as the
___ end, and the opposite end of the same strand, with the deoxyribose sugar, is referred to
as the ___ end.

A

5’; 3’

71
Q

Bases on _________ strands of DNA hydrogen bond to one another to form ______________ DNA molecule

A

opposite; double-stranded

72
Q

G (guanine) forms __ hydrogen bonds
with C (cytosine), and A (adenine) forms __ hydrogen bonds with T (thymine).

A

3; 2

73
Q

As base pairs form between two strands of DNA, the molecule is twisted into a double ____

A

helix

74
Q

RNA takes on a greater _______ of structures. RNA structures include relatively short _____ forms, as well as structures that ____ back on themselves in clover or hairpin formations.

A

variety; linear; fold

75
Q

Nucleotides perform many functions in cells, in addition to serving as the _______ ______ of nucleic acids.

A

building blocks

76
Q

Two nucleotides in particular, adenosine triphosphate (ATP) and guanosine triphosphate (GTP), are the primary molecules that ________ chemical energy from one ________ system to another. These nucleotides also regulate and adjust _______ activity.

A

transport; reaction; cellular

77
Q

4 major types of biological molecules:

A

carbohydrates, lipids, proteins, and
nucleic acids.

78
Q

What groups of atoms are found in amino acids?

A

All amino acids contain an amine group, carboxylic acid, and an R group.

79
Q

Describe the difference between the primary and secondary protein structures.

A

Primary protein structure is linear sequence of order of amino acids.

Secondary protein structure is the result of hydrogen bonding between different parts of the same amino acid backbone.

80
Q

Explain why it is necessary for a protein to adopt specific tertiary and quaternary arrangements.

A

For proteins to function properly, they need to fold into very specific 3D shapes (tertiary structure) and may require the assembly of multiple polypeptides (quaternary structure).

81
Q

Explain the role of hydrogen bonding and disulfide bonds between R groups.

A

Hydrogen and disulfide bonds help to maintain proper secondary and tertiary structure—i.e., they are responsible for the shape of the polypeptide.

82
Q

List some of the different types of proteins and their functions. Identify specific applications of these proteins in various living organisms.

A

Structural proteins provide framework support. Examples in animals are spider web silk proteins and eggshells. Defensive proteins fight off infection. Examples in animals are antibodies. Signal proteins are chemical messengers. Examples in animals are hormones.

83
Q

Relate the diversity in protein structure to the diversity in its function.

A

There are 20 different amino acids. They represent an almost limitless number of combinations for different proteins.

This factor and the ability of amino acids along the backbone of a protein molecule to make various combinations of hydrogen, disulfide bonds, and non-polar configurations leads to tremendous diversity of shape of proteins and therefore function.

84
Q

What is the role of the sugar and phosphate groups in the structure of nucleic acids?

A

Sugar and phosphate groups form the backbone of a nucleic acid molecule.

85
Q

Explain the similarities and differences between DNA and RNA.

A

DNA is double stranded and RNA is a single stranded molecule. Nitrogenous bases in DNA are G (guanine), A (adenine), T (thymine), C (cytosine) Nitrogenous bases in RNA are G, A, U (uracil), and C. DNA almost always forms a double helix while RNA can take on a variety of configurations.

86
Q

How does the function of nucleic acids differ from that of other types of macromolecules?

A

Other macromolecules have a large number of structures and functions.

Nucleic acids have only one function – working together to make proteins.

87
Q

Your biology teacher tells you that nucleic acids, fatty acids, and amino acids can increase the H+ concentration of a solution. Explain how this is possible.

A

When nucleotides contain at least one phosphate group and they break down, they produce phosphoric acid.

Fatty acids break down and produce ketone bodies that are acidic.

Amino acids containing sulfur in their R group will produce sulfuric acid when they break down.

In each case, there is a change in the concentration of hydrogen ions in solution.

88
Q

proteins

A

carry out vital structural and functional roles

89
Q

what are proteins made of?

A

proteins are polymers that are made up of amino acid monomers

90
Q

amino acid

A

a molecule that consists of a carboxyl group and an amino group; building blocks of proteins.

91
Q

essential amino acids

A

amino acids that need
to be acquired through diet (8 amino acids)

92
Q

Non-Essential Amino Acids

A

amino acids that can be made in the body (12 amino acids)

93
Q

protein

A

large molecules made up of amino acids with a distinct 3D shape

94
Q

building proteins

A

Proteins are built by attaching Amino Acids
into chains

Amino acids are connected by attaching a NH2
group to a COOH group by Dehydration
Synthesis

The resulting bond is called a Peptide Bond

95
Q

peptide

A

a term used to describe a chain of amino acids

96
Q

polypeptide

A

a peptide with more than 50 amino acids

97
Q

primary structure

A

chain of amino acids

Changing even ONE
amino acid in the chain
can alter/destroy the
final structure/function
of the protein

98
Q

second structure

A

the coiling/folding of
amino acid chains

Occurs because of hydrogen bonding between different amino acids

99
Q

tertiary structure

A

folding of protein caused by
R-group interactions

100
Q

quaternary structure

A

linking several separate
polypeptide chains

101
Q

What causes proteins to no longer function?

A

changes in pH and temp can alter the shape of proteins causing them to no longer function

102
Q

denaturation

A

the loss of both the structure and function of a protein

103
Q

True or false

Proteins can also bond with non-protein structures

A

true

104
Q

How does hemoglobin carry oxygen?

A

Hemoglobin carries oxygen with the help of four Heme Groups
which contain Iron

105
Q

Nucleic acids

A

Nucleic Acids serve as the assembly instructions for all proteins in living organisms.

Two types: DNA and RNA

DNA stores hereditary information

RNA is involved in protein synthesis and is the
hereditary molecule of some viruses

106
Q

Nucleotides

A

All nucleic acids are
polymers of nucleotides

Nucleotides consists of
a sugar, phosphate
group, and a
nitrogenous base

107
Q

DNA and RNA are chains of nucleotides, joined together by the ________ and the
______ by _____________

A

phosphate; sugar; phosphodiester bonds

108
Q

DNA molecules are _________, contains nitrogen bases A,T,G,C, and _________ sugar

A

double stranded; deoxyribose

109
Q

RNA molecules are __________, contains nitrogen bases A,U,G,C, and ______ sugar

A

single stranded; ribose

110
Q

Adenosine triphosphate (ATP) and Guanosine triphosphate (GTP) are that _________that transport energy from one ______ system to another

A

nucleotides; reaction

Biology 12U (45 decks)

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