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Kin 267 (Phys. 1) > Chapter 2 (pt. 2: amino acids and protein) > Flashcards

Chapter 2 (pt. 2: amino acids and protein) Flashcards

1
Q

What are the monomers of proteins?

A

Amino acids.

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2
Q

How many different amino acids exist?

A

20

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3
Q

What are the three important functional groups attached to the central carbon atom of an amino acid?

A

1) Amino group (—NH2), 2) Acidic carboxyl group (—COOH), 3) Side chain (R group).

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4
Q

How are the amino and carboxyl groups of amino acids affected at normal body pH?

A

They are both ionized.

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5
Q

What gives each amino acid its distinctive chemical identity?

A

The different side chains (R groups).

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6
Q

What distinguishes glycine among amino acids?

A

It is the simplest amino acid, with a side chain that is just a hydrogen atom.

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7
Q

What is unique about cysteine?

A

It contains sulfur in its side chain and is one of only two amino acids with this element.

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8
Q

Describe the structure of tyrosine.

A

It has a side chain that contains a six-carbon aromatic ring.

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9
Q

What characteristic does lysine have?

A

It has an additional amino group at the end of its side chain, which gives it basic properties.

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10
Q

What are structural proteins?

A

Proteins that form the framework of body parts.

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11
Q

Give two examples of structural proteins and their locations.

A

Collagen (in bones and connective tissues) and keratin (in skin, hair, and nails).

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12
Q

What do regulatory proteins do?

A

They act as hormones and neurotransmitters to regulate body processes and growth.

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13
Q

Name two examples of regulatory proteins and their functions.

A

Insulin (regulates blood glucose) and Substance P (mediates pain).

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14
Q

What is the function of contractile proteins?

A

They enable muscle contraction and movement.

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15
Q

Give two examples of contractile proteins.

A

Myosin and actin.

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16
Q

What are immunological proteins responsible for?

A

They help protect the body from foreign substances and pathogens.

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17
Q

Name two examples of immunological proteins.

A

Antibodies and interleukins.

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18
Q

What is the role of transport proteins?

A

They carry essential substances throughout the body.

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19
Q

Provide an example of a transport protein.

A

Hemoglobin (transports oxygen and carbon dioxide).

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20
Q

What are catalytic proteins also known as?

A

Enzymes

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21
Q

Name two examples of catalytic proteins.

A

Salivary amylase and sucrase.

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22
Q

How are proteins synthesized?

A

By sequentially joining amino acids through peptide bonds.

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23
Q

Describe how a peptide bond is formed.

A

A covalent bond forms between the carbon in the carboxyl group of one amino acid and the nitrogen in the amino group of another, releasing a molecule of water (dehydration synthesis).

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24
Q

What is the process of breaking a peptide bond called?

A

Hydrolysis reaction, as seen during protein digestion.

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25
Q

What are essential (indispensable) amino acids?

A

Amino acids that cannot be synthesized by the human body in sufficient amounts and must be included in the diet.

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26
Q

Why are essential amino acids important?

A

necessary for various bodily functions and must come from dietary sources.

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27
Q

What are nonessential (dispensable) amino acids?

A

Amino acids that can be synthesized by the human body in sufficient amounts to meet its needs.

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28
Q

What is leucine and where can it be found?

A

Leucine is an essential amino acid found in dairy products that the body cannot synthesize on its own.

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29
Q

Can nonessential amino acids be obtained from the diet?

A

Yes, while the body can synthesize them, they can also be obtained through dietary sources.

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30
Q

Why is it important to consume essential amino acids?

A

They are necessary for building muscle and various bodily functions.

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31
Q

What is the benefit of consuming nonessential amino acids?

A

While the body can synthesize them, consuming them can still contribute to overall amino acid intake.

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32
Q

Which amino acid is most essential for muscle protein synthesis?

A

Leucine

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33
Q

Should branch-chain amino acids be a focus in supplementation?

A

While not as beneficial for some goals, prioritizing essential amino acids like leucine for muscle building is important.

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34
Q

How many essential amino acids are there?

A

9 essential amino acids.

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35
Q

How many non-essential amino acids are there?

A

11 non-essential amino acids.

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36
Q

What are conditionally essential amino acids?

A

Amino acids that can be produced by the body but are better obtained through diet during certain conditions.

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37
Q

How many conditionally essential amino acids are there?

A

3 conditionally essential amino acids.

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38
Q

Why might conditionally essential amino acids be important to consume?

A

During times of stress, illness, or recovery, the body’s demand may exceed its ability to produce them.

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39
Q

what does each amino acid contain?

A

Each amino acid contains a central carbon atom bound to a hydrogen atom, an amino group, an acid group, and a side chain.

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40
Q

what is the amino acid pool?

A

All of the amino acids in body tissues and fluids that are available for use by the body.

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41
Q

what is protein turnover?

A

The continuous synthesis and breakdown of body proteins.

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42
Q

What is the amino acid pool used for?

A

The amino acid pool is used to synthesize protein and non-protein molecules.

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43
Q

Where does the amino acid pool come from?

A

The amino acid pool comes from dietary proteins and the breakdown of existing body proteins.

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44
Q

How can amino acids be utilized for energy?

A

Amino acids can be broken down for energy.

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45
Q

Besides energy, what else can amino acids be used to synthesize?

A

Amino acids can be used to synthesize glucose or fatty acids.

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46
Q

What non-protein molecules can be synthesized from amino acids?

A

Amino acids can be used to synthesize non-protein molecules such as DNA or RNA.

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47
Q

Can the body store amino acids like glucose or fatty acids?

A

No, the body cannot store amino acids like glucose or fatty acids; they can only be stored as body proteins, which are continuously broken down and used.

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48
Q

function of protein in the body:

A

Proteins give structure to the body, regulate processes, provide protection, assist in muscle contraction, transport substances, and serve as enzymes

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49
Q

What is a peptide bond?

A

A peptide bond is a chemical bond that links amino acids together.

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50
Q

How is a peptide bond formed?

A

A peptide bond is formed between the acid group of one amino acid and the nitrogen group of the next amino acid.

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51
Q

What is a dipeptide bond?

A

A dipeptide bond is a bond formed between two amino acids.

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52
Q

What is a polypeptide?

A

A polypeptide is a chain formed from many amino acids (10 or more).

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53
Q

What is a protein made of?

A

A protein is made of one or more polypeptide chains folded into a three-dimensional shape, which determines its function.

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54
Q

How is a dipeptide formed?

A

A dipeptide is formed when two amino acids combine.

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55
Q

What happens when more amino acids are added to a dipeptide?

A

Adding more amino acids creates tripeptides, chain-like peptides (4–9 amino acids), or polypeptides (10–2000+ amino acids).

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56
Q

What is the structure of a small protein?

A

Small proteins consist of a single polypeptide chain with a minimum of 50 amino acids.

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57
Q

What is the structure of larger proteins?

A

Larger proteins can have hundreds or thousands of amino acids and may comprise multiple folded polypeptide chains.

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58
Q

How does the variation in amino acid number or sequence affect proteins?

A

Each variation in the number or sequence of amino acids results in a different protein.

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59
Q

How are amino acids similar to alphabet letters?

A

Amino acids are like alphabet letters, and their combinations create diverse peptides, polypeptides, and proteins.

60
Q

What is the primary structure of a protein?

A

The primary structure is the linear sequence of amino acids in a protein, linked by covalent peptide bonds. This sequence is genetically determined.

61
Q

What can happen if the primary structure of a protein is altered?

A

Alterations in the primary structure can affect the protein’s function, as seen in sickle cell disease, where a mutation changes hemoglobin’s structure, causing blood cells to deform.

62
Q

What is a covalent peptide bond?

A

A covalent peptide bond is a chemical link formed between two amino acids in a protein.

63
Q

What is the secondary structure of a protein?

A

The secondary structure involves the local folding of the polypeptide chain into shapes like alpha helices (spiral shapes) and beta sheets (zig-zag patterns), stabilized by hydrogen bonds.

64
Q

How are secondary structures like alpha helices and beta sheets held together?

A

They are held together by hydrogen bonds.

65
Q

What is the tertiary structure of a protein?

A

The tertiary structure is the overall three-dimensional shape of a polypeptide, formed by interactions like hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

66
Q

What is the quaternary structure of a protein?

A

The quaternary structure involves multiple polypeptide chains arranged together, held by interactions similar to those in the tertiary structure.

67
Q

What are fibrous proteins and their function?

A

Fibrous proteins are insoluble in water, form long strands, and have structural roles (e.g., collagen, keratin).

68
Q

What are globular proteins and their function?

A

Globular proteins are soluble in water, spherical, and perform metabolic functions (e.g., enzymes, antibodies).

69
Q

What is denaturation, and how can it happen?

A

Denaturation is when proteins lose their functional shape due to environmental changes, such as heat (like cooking an egg), disrupting their function.

70
Q

Primary Structure

A

This is the linear sequence of amino acids in a polypeptide chain, connected by peptide bonds.

71
Q

Secondary Structure

A

The local folding of the polypeptide chain into alpha helices (spiral shapes) and beta sheets (zig-zag patterns), stabilized by hydrogen bonds between amino acids.

72
Q

Tertiary Structure

A

The overall three-dimensional shape of a single polypeptide chain, formed through interactions like hydrogen bonds, ionic bonds, and disulfide bridges.

73
Q

Quaternary Structure

A

The arrangement of two or more polypeptide chains, coming together to form a functional protein complex.

74
Q

list the types of protien:

A

Structural: Form structural framework of various parts of body.

Regulatory: Function as hormones that regulate various physiological processes

Contractile: Allow shortening of muscle fibers (cells) which produces movement.

Immunological: Aid responses that protect body against foreign substances and invading pathogens.

Transport: Carry vital substances throughout body.

Catalytic: Act as enzymes that regulate biochemical reactions.

“Some Really Cool Iguanas Travel Constantly.”

75
Q

Where does transcription occur during protein synthesis?

A

Transcription occurs in the nucleus.

76
Q

What is produced during transcription?

A

Messenger RNA (mRNA) is produced during transcription.

77
Q

What happens to mRNA after it is made?

A

The mRNA leaves the nucleus and travels to the cytoplasm, where it attaches to a ribosome.

78
Q

Where does translation take place in the cell?

A

Translation takes place in the cytosol.

79
Q

What does the ribosome do during translation?

A

The ribosome reads the mRNA code three nucleotides at a time (codon) and helps assemble the corresponding amino acids.

80
Q

What molecule brings amino acids to the ribosome?

A

Transfer RNA (tRNA) brings amino acids to the ribosome.

81
Q

What is a codon?

A

A codon is a set of three nucleotides on mRNA that corresponds to a specific amino acid.

82
Q

How are amino acids linked together during translation?

A

Amino acids are linked together to form a polypeptide chain.

83
Q

What happens to the polypeptide chain after translation?

A

The polypeptide chain folds to become a functional protein.

84
Q

What does nitrogen balance measure?

A

Nitrogen balance measures the balance between the amount of nitrogen you consume and the amount your body gets rid of.

85
Q

How do you get nitrogen into your body?

A

You get nitrogen mostly from the protein in the food you eat.

86
Q

How does your body lose nitrogen?

A

Your body loses nitrogen through urine, feces, sweat, and other bodily processes.

87
Q

What is positive nitrogen balance?

A

Positive nitrogen balance occurs when you take in more nitrogen than you lose, indicating your body is building more proteins than it is breaking down.

88
Q

When is positive nitrogen balance commonly seen?

A

Positive nitrogen balance is common during periods of growth, such as in children, pregnant women, or bodybuilders building muscle.

89
Q

What is negative nitrogen balance?

A

Negative nitrogen balance happens when your body loses more nitrogen than it consumes, suggesting your body is breaking down more protein than it is building.

90
Q

When might negative nitrogen balance occur?

A

Negative nitrogen balance can occur during illness, malnutrition, or periods of stress.

91
Q

What is balanced nitrogen?

A

Balanced nitrogen occurs when nitrogen intake equals nitrogen loss, indicating a stable state.

92
Q

When is balanced nitrogen typically desired?

A

Balanced nitrogen is typically desired for maintaining overall health in adults who are not growing or recovering from illness.

93
Q

what does DNA form and regulate?

A

D N A forms the genetic code in the nuclei of body cells and it regulates most of the cell’s activities.

94
Q

what does RNA guide?

A

protein formation

95
Q

What elements do nucleic acids contain?

A

Carbon, hydrogen, oxygen, nitrogen, and phosphorus.

96
Q

What are the two types of nucleic acids?

A

DNA (Deoxyribonucleic acid) and RNA (Ribonucleic acid).

97
Q

What is the role of DNA in cells?

A

DNA is the genetic material that determines inherited traits and controls protein production, passing on genetic information during cell division.

98
Q

How does RNA function in relation to DNA?

A

RNA carries instructions from DNA to guide cells in making proteins from amino acids.

99
Q

What happens to DNA when cells divide?

A

DNA passes on genetic information to the new cells.

100
Q

Why is protein production important in cells?

A

Proteins help regulate what happens in body cells.

101
Q

What are the repeating units that make up nucleic acids?

A

Nucleotides

102
Q

What are the three components of each nucleotide in DNA?

A

A nitrogenous base, a pentose sugar, and a phosphate group.

103
Q

Name the four nitrogenous bases found in DNA.

A

Adenine (A), Guanine (G), Thymine (T), and Cytosine (C).

104
Q

Which nitrogenous bases in DNA are purines?

A

Adenine (A) and Guanine (G).

105
Q

Which nitrogenous bases in DNA are pyrimidines?

A

Thymine (T) and Cytosine (C).

106
Q

What sugar is found in the nucleotides of DNA?

A

Deoxyribose, a five-carbon sugar.

107
Q

What role do phosphate groups play in the structure of DNA?

A

They form the “backbone” of the DNA strand by linking with pentose sugars.

108
Q

How do the bases A, T, C, and G contribute to the structure of DNA?

A

They pair up to hold the DNA strands together.

109
Q

Describe the “backbone” of a DNA strand.

A

It is composed of alternating pentose sugars and phosphate groups

110
Q

What is the structure of a DNA molecule?

A

DNA is arranged in a double helix.

111
Q

What stabilizes the structure of the DNA helix?

A

Hydrogen bonds between each base pair stabilize the helix.

112
Q

What is the function of DNA in human cells?

A

DNA forms the inherited genetic material inside each human cell.

113
Q

Who proposed the structure of DNA and when?

A

F.H.C. Crick and J.D. Watson in 1953.

114
Q

What does the double helix model of DNA resemble?

A

A spiral ladder.

115
Q

What does the double helix model of DNA resemble?

A

A spiral ladder.

116
Q

What forms the sides of the DNA ladder?

A

Alternating phosphate groups and deoxyribose sugars.

117
Q

What forms the rungs of the DNA ladder?

A

Paired bases bonded by hydrogen bonds.

118
Q

Which bases pair together in DNA?

A

Adenine pairs with thymine, and cytosine pairs with guanine.

119
Q

What is complementary base pairing?

A

Knowing the sequence of one DNA strand allows prediction of the complementary strand.

120
Q

What happens during DNA replication?

A

DNA strands unwind, and each serves as a template for a new complementary strand.

121
Q

What are mutations?

A

Changes in the DNA sequence.

122
Q

What can mutations lead to?

A

They can lead to cell death, cancer, or genetic defects.

123
Q

What is the key structural difference between RNA and DNA in humans?

A

RNA is single-stranded, while DNA is double-stranded.

124
Q

What type of sugar is found in RNA?

A

Ribose.

125
Q

Which base does RNA contain that DNA does not?

A

Uracil (U) instead of thymine (T).

126
Q

What is the primary function of messenger RNA (mRNA)?

A

It carries genetic instructions from DNA.

127
Q

What role does ribosomal RNA (rRNA) play in cells?

A

It forms part of the ribosome and aids in protein synthesis.

128
Q

How do RNA types contribute to the process of protein synthesis?

A

Each type of RNA plays a part in translating DNA’s instructions into proteins.

129
Q

What is the function of transfer RNA (tRNA)?

A

It brings amino acids to the ribosome for protein assembly.

130
Q

How do you differentiate between DNA and RNA bases in terms of thymine and uracil?

A

DNA contains thymine (T), whereas RNA contains uracil (U).

131
Q

What is the primary role of adenosine triphosphate (ATP) in living organisms?

A

ATP is the primary energy carrier in all living organisms.

132
Q

Name one cellular process powered by ATP.

A

Muscle contractions.

133
Q

Give another example of a cellular activity that requires ATP.

A

Cell division.

134
Q

How does ATP contribute to movements within cells?

A

It provides the energy needed for intracellular movement.

135
Q

What role does ATP play in cellular transportation?

A

It transports substances across cell membranes.

136
Q

How does ATP assist in metabolism related to building larger molecules?

A

It provides the energy required for building larger molecules.

137
Q

Describe the structural components of ATP.

A

ATP consists of three phosphate groups attached to adenosine, which includes adenine and the sugar ribose.

138
Q

What is the primary process cells use to produce ATP?

A

The breakdown of glucose during cellular respiration.

139
Q

What are the two phases of cellular respiration?

A

The anaerobic phase and the aerobic phase.

140
Q

Where does the anaerobic phase occur in the cell, and does it require oxygen?

A

It occurs in the cytoplasm and does not require oxygen.

141
Q

What is the main product of glucose breakdown during the anaerobic phase?

A

Pyruvic acid.

142
Q

How many ATP molecules are produced per glucose molecule during the anaerobic phase?

A

2 ATP molecules.

143
Q

In which part of the cell does the aerobic phase occur, and what does it require?

A

It occurs in the mitochondria and requires oxygen.

144
Q

What are the end products of glucose breakdown during the aerobic phase?

A

Carbon dioxide and water.

145
Q

How many ATP molecules are generated per glucose molecule in the aerobic phase?

A

30 to 32 ATP molecules.

146
Q

Why is the anaerobic phase of cellular respiration considered to occur quickly?

A

Because it does not require oxygen.

Kin 267 (Phys. 1) (7 decks)

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