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GRADE 11 > GEN BIO: PROTEINS and NUCLEIC ACIDS > Flashcards

GEN BIO: PROTEINS and NUCLEIC ACIDS Flashcards

1
Q

From the Greek word proteios, meaning “first place,” suggests the importance of this class of macromolecules

A

Proteins

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2
Q

6 BIOLOGICAL FUNCTIONS OF PROTEINS

A
  • Enzymes – Ribonuclease
  • Regulatory proteins – Insulin
  • Transport proteins – Hemoglobin
  • Structural proteins – Collagen
  • Contractile proteins – Actin, Myosin
  • Exotic proteins – Antifreeze proteins in fish
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3
Q

OTHER TYPES OF PROTEINS

A
  • DEFENSIVE PROTEINS
  • SIGNAL PROTEINS
  • RECEPTOR PROTEINS
  • STORAGE PROTEINS
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4
Q

Type of Protein. Antibodies of the immune system

A
  • DEFENSIVE PROTEINS
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5
Q

Type of Protein. many of the hormones and other messengers that help coordinate body activities by communicating between cells

A
  • SIGNAL PROTEINS
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6
Q

Type of Protein. may be built into cell membranes and transmit signals into cells

A
  • RECEPTOR PROTEINS
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7
Q

Type of Protein. such as ovalbumin, the protein of egg white, which serves as a source of amino acids for developing embryos

A
  • STORAGE PROTEINS
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8
Q

Probably the most important role for proteins is as __________

A

Enzymes

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9
Q

biological catalysts that speed and regulate virtually all chemical reactions in cells

A

Enzymes

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10
Q

found in hair and the fibers that make up connective tissues such as tendons and ligaments.

A

STRUCTURAL PROTEINS

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11
Q

Muscles contain _______ and __________ proteins.

A

contractile; regulatory

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12
Q

Contractile Proteins (2)

A

Myosin and Actin; functions in shortening the muscle fibers

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13
Q

Contractile Proteins (2)

A

Myosin and Actin; function in shortening the muscle fibers

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14
Q

Regulatory Proteins (2)

A

Tropomyosin and Troponin
- starts and stops shortening of muscle cell
- troponin moves tropomyosin off the actin active sites

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15
Q

Muscle contraction is activated by the release of calcium into sarcoplasm and its binding to troponin. With what type of protein?

A

Regulatory PRotein=Tropomyosin and Troponin

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16
Q

Regulatory Protein formed in pancreatic tissue that helps to regulate blood sugar level

A

Insulin

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17
Q

Other proteins called _________ regulate biosynthesis of enzymes

A

Repressors

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18
Q

Proteins that protect against disease

A

Defensive Proteins

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19
Q

A ________ is a protein molecule usually found embedded within the plasma membrane surface of a cell that receives chemical signals from outside the cell and when such chemical signals bind to a receptor, they cause some form of cellular/tissue response.

A

Receptor

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20
Q

Functions in storage of amino acids

A

Storage Proteins

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21
Q

Protein in Milk

A

Casein

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22
Q

Exotic Proteins

A
  • Monelin
  • Antifreeze
  • Resillin
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23
Q

Protein of an African plant has an intensely sweet taste and used as non toxic food sweetener for human use

A

Monelin

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24
Q

Protein present in wing hinges of some insects with elastic properties

A

Resillin

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25
Q

PROTEINS ARE MADE FROM AMINO ACIDS LINKED BY ________ BONDS

A

PEPTIDE

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26
Q

Protein diversity is based on differing arrangements of a common set of just _______ amino acids.

A

20

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27
Q

Amino acids all have an ______ and a _______ group

A

amino group; carboxyl

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28
Q

These functional groups (amino and carboxyl) are covalently bonded to a central carbon atom, called the ________

A

alpha carbon.

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29
Q

Also bonded to the alpha carbon is a ________ and a chemical group symbolized by the ____.

A

hydrogen atom; letter R

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30
Q

the simplest amino acid; the R group is just a hydrogen atom

A

Glycine

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31
Q

structure of the ________ determines the specific properties of each of the 20 amino acids that are found in proteins.

A

R group

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32
Q

Aspartate doesn’t have _____ compared to aspartic

A

H atom

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33
Q

________ residues function in many enzyme-catalyzed reactions as proton donors and/or acceptors

A

Histidine

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34
Q

Amino acids with ___________ help proteins dissolve in the aqueous solutions inside cells

A

polar and charged R groups

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35
Q

Cells join amino acids together in a dehydration reaction that links the carboxyl group of one amino acid in the amino group of the next acid as a water molecule is removed. The resulting covalent linkage is called a _____________

A

peptide bond.

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36
Q

The product of the reaction from two amino acids is a ________

A

dipeptide.

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37
Q

Chain of amino acids

A

Polypeptide

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38
Q

The beginning amino group in a dipeptide

A

Terminal Amino Group (N-Terminal)

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39
Q

The end group in a Dipeptide

A

Terminal Carboxyl Group (C-Terminal)

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40
Q

Most polypeptides are at least how many amino acids in length?

A

100

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41
Q

T or F. Each polypeptide has a unique sequence of amino acids.

A

T

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42
Q

one or more polypeptide chains precisely coiled, twisted, and folded into a unique three-dimensional shape.

A

Proteins

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43
Q

A protein’s _______ determines its function

A

specific shape

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44
Q

a process where polypeptide chains unravel, losing their specific shape and as a result, their function

A

Denaturation

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45
Q

Causes of Denaturation

A

Change in salt concentration, pH, excessive heat

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46
Q

4 levels of structure for protein shape

A

Primary
Secondary
Tertiary
Quaternary

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47
Q

a protein’s unique sequence of amino acids

A

Primary Structure

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48
Q

T or F. Even a slight change in a protein’s primary structure may affect its overall shape and its ability to function

A

T

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49
Q

parts of the polypeptide coil or fold into local patterns called _______

A

Secondary Structure

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50
Q

In Secondary Structure, coiling results in a ________ and certain kinds of folding leads to a________

A

alpha helix; beta pleated sheet

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51
Q

T or F. Beta Pleated sheets are found in fibrous and globular protein

A

T

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52
Q

What stabilizes the B-pleated sheet?

A

hydrogen bonds between peptide bonds

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53
Q

Both alpha helix and beta pleated sheets are maintained by regularly spaced __________between the hydrogens of the –N-H groups and the oxygens of the –C=O groups of neighboring peptide bonds along the polypeptide chain

A

hydrogen bonds

54
Q

Many fibrous proteins, such as the structural protein of hair, have the ________ structure over most of their length

A

alpha-helix

55
Q

_________ make up the core of many globular proteins

A

Pleated sheets

56
Q

refers to the overall three-dimensional shape of a polypeptide

A

Tertiary Structure

57
Q

Most _________can be roughly described as either globular or fibrous. Generally, results from interactions among the R groups of the amino acids making up the polypeptide

A

tertiary structures

58
Q
  • Many proteins consist of two or more polypeptide chains or subunits. Such proteins have a ________, resulting from the association of the subunits.
A

quaternary structure

59
Q

infectious misshapen proteins that are associated with serious degenerative brain diseases such as mad cow disease.

A
  • Prions
60
Q

diseases such as Alzheimer’s and Parkinson’s involve an accumulation of _______

A

misfolded proteins.

61
Q

The amino acid sequence of a polypeptide is programmed by a discrete unit of inheritance known as

A

gene.

62
Q

Genes consist of __________, one of the two types of polymers known as nucleic acids.

A

DNA (deoxyribonucleic acid)

63
Q

A gene does not put its genetic DNA information to work directly. It works through an intermediary –the second type of nucleic acid known as _________.

A

ribonucleic acid (RNA)

64
Q

The monomers that make up nucleic acid

A

nucleotides.

65
Q

nucleotide has three parts

A

-A five-carbon sugar (DNA has deoxyribose, whereas RNA has ribose)
-Linked to one side of the sugar is a phosphate group
-Linked to the sugar’s other side is a nitrogenous base

66
Q

DNA nucleotide vs. RNA nucleotide

A

DNA - has Thymine
- doesn’t have O in carbon 2

RNA - has Uracuk
- has O in carbon 2

67
Q
  • Like polysaccharides and polypeptides, a nucleic acid polymer-a ___________-forms from its monomers by __________ reactions.
A

polynucleotide; dehydration

68
Q

T or F. The phosphate group of one nucleotide bonds to the phosphate of the next monomer. result is a repeating sugar-phosphate backbone in the polymer.

A

F. The phosphate group of one nucleotide bonds to the sugar of the next monomer.

69
Q

DNA is a double helix, in which __________ wrap around each other.

A

two polynucleotides

70
Q

T or F. nitrogenous bases protrude from the two sugar-phosphate backbones into the center of the helix in DNA

A

T

71
Q

A certain purine can only pair with a certain pyrimidine. A pairs with T, and C pairs with G. This is known a base complementary rule or _______.

A

Chargaff’s Rule

72
Q

T or F. Two DNA chains are held in a double helix by hydrogen bonds between their paired bases.

A

T

73
Q

Every base pair in the double helix is separated from the next base pair by _____nm.

A

0.34 nm

74
Q

The two strands of the double helix run in opposite directions (__________ orientation)

A

antiparallel

75
Q

mainly involved in the process of protein synthesis under the direction of DNA.

A

RNA

76
Q

Usually single-stranded and is made of ribonucleotides

A

RNA

77
Q

Ribonucleotide in the RNA chain contains_________(the pentose sugar), one of the four nitrogenous bases (A, U, G, and C) and the phosphate group.

A

ribose

78
Q

4 major types of RNA:

A
  1. messenger RNA (mRNA)
  2. ribosomal RNA (rRNA)
  3. transfer RNA (tRNA)
  4. microRNA (miRNA)
79
Q

carries the message from DNA, which controls all of the cellular activities

A

messenger RNA

80
Q

major constituent of ribosomes on which the mRNA binds

A

ribosomal RNA

81
Q

ensures the proper alignment of the mRNA and the ribosomes

A

ribosomal RNA

82
Q

has enzymatic activity and catalyzes the formation of the peptide bonds between two aligned amino acids

A

ribosomal RNA

83
Q

Polymers of amino acids arranged in a linear sequence

A

Proteins

84
Q

Enzymes that break down their substrates

A

Catabolic Enzymes

85
Q

Enzymes that build more complex molecules from their substrates are called?

A

Anabolic Enzymes

86
Q

Enzymes that affect the rate of reaction are called?

A

Catalytic Enzymes

87
Q

In every reaction, an enzyme will bind with a substrate in an area on the enzyme’s surface called the _______, forming a substrate-enzyme complex.

A

Active Site

88
Q

An enzyme which hydrolyzes its substrate amylose, a component of starch

A

Salivary Amylase

89
Q

Each enzyme is specific for the substrate (a reactant that binds to an enzyme) it acts on, such that their active sites have very precise shapes, that only, one substrate can fit in each site and is chemically attracted
to it. This is known as

A

Enzyme-Substrate Specificity

90
Q

rates of enzyme reactions are also affected by different factors such as

A

temperature, pH, and amount of substrate.

91
Q

T or F. chemical reactions increase as temperature increases

A

T. chemical reactions increase as temperature increases because the reacting molecules move faster and collide more often.

92
Q

However, as the temperature continues to increase beyond the optimum temperature, ___________
occurs: chemical bonds of the enzymes break causing alteration in the shape of the active site until it is no longer complementary to the substrate molecule.

A

enzyme denaturation

93
Q

T or F. s. Most enzymes in the human body have optimum temperature at 37.0 ‘C. But some enzymes in organisms that live in extreme conditions, like those
in bacteria which thrive in hot springs or hydrothermal vents, can have extreme optimum temperatures of more than 65”C.

A

T

94
Q

T or F. pH, which indicates the acidity/basicity of a solution, actually measures the concentration of hydrogen ions (H+). The lower the pH, the higher the concentration of H+ ions there is.

A

T.

94
Q

T or F. pH, which indicates the acidity/basicity of a solution, actually measures the concentration of hydrogen ions (H+). The lower the pH, the higher the concentration of H+ ions there is.

A

T.

95
Q

Most enzymes found in the human body have optimum
pH between pH ____

A

6-8

96
Q

T or F. enzyme activity decreases as substrate concentration increases

A

F. Increases

97
Q

Active sites of enzymes is said to be saturated with the substrate and thus called the _____

A

saturation point

98
Q

monomers that make up proteins

A

Amino Acids

99
Q

Structure of amino acid

A
  • central carbon atom (alpha carbon)
  • amino group
  • carboxyl group
  • hydrogen atom
  • R-group
100
Q

______ is an exception to the standard structure of amino acid, since its amino group is not separate from the side chain

A

Proline

101
Q

Amino acids are represented by a _________

A

single upper case letter or a three-letter abbreviation

102
Q

___________ and ________ in the polypeptide chain ultimately determine the protein’s shape, size, and function.

A

amino acid sequence and the number of amino acids

103
Q

products formed by such linkages (peptide bonds) are called ______

A

peptides; polypeptides as more amino acids join

104
Q

After protein synthesis (translation), most proteins are modified. These are known as ______

A

post-translational modifications

105
Q

The unique sequence for every protein is ultimately determined by the _____ encoding the protein.

A

gene

106
Q

The local folding of the polypeptide in some regions

A

Secondary Structure

107
Q

The a-helix and b-pleated sheet are secondary structures of proteins that form because of ________ between carbonyl and amino groups in the
peptide backbone.

A

hydrogen bonding

108
Q

Every helical turn in an alpha helix has ______ amino acid residues.

A

3.6

109
Q

T or F. In the b-pleated sheets, the pleated segments align parallel or antiparallel to each other, and hydrogen bonds form between the partially positive nitrogen
atom in the amino group and the partially negative oxygen atom in the carbonyl group of the peptide backbone.

A

T

110
Q

The a-helix and B-pleated sheet structures are found in most ____ and _____, and they play an important structural role.

A

globular and fibrous proteins

111
Q

When protein folding takes place, the hydrophobic R groups of nonpolar amino acids lay in the interior of the protein, whereas the hydrophilic R groups lay on the outside. The former types of interactions are also known as __________

A

hydrophobic interactions

112
Q

In nature, some proteins are formed from several polypeptides (each polypeptide is called a subunit), and the interaction of these subunits forms
the ________

A

quaternary structure.

113
Q

T or F. Not all proteins are denatured at high temperatures;

A

T. Not all proteins are denatured at high temperatures; for instance, bacteria that survive in hot springs have proteins that function at temperatures close to boiling. The stomach is also very acidic, has a low pH, and denatures proteins as part of the digestion process; however, the digestive enzymes of the stomach retain their activity under these conditions

114
Q

Protein folding is critical to its function. It was originally thought that the proteins themselves were responsible for the folding process. Only recently was it found that often they receive assistance in the folding process from protein helpers known as_________that associate with the target protein during the folding process. They act by preventing aggregation of polypeptides that make up the complete protein structure and they disassociate from the protein once the target protein is folded.

A

chaperones (or.chaperonins)

115
Q

_______ are the most important macromolecules for the continuity of life. They carry the genetic blueprint of a cell and carry instructions for the functioning of the cell.

A

Nucleic acids

116
Q

T or F. In prokaryotes, the DNA is not enclosed in a membranous envelope, unlike eukaryotes.

A

T

117
Q

In eukaryotic cells but not in prokaryotes, DNA forms a complex with histone proteins to form _______, the substance of eukaryotic chromosomes.

A

chromatin

118
Q

The DNA molecules never leave the nucleus, but, use an intermediary to communicate with the rest of the cell instead. This intermediary is the ______

A

messenger RNA (mRNA).

119
Q

Other types of RNA-like rRNA IRNA,
and microRNA-are involved in ______ and _____

A

protein synthesis and its regulation.

120
Q

The nitrogenous bases, important components of nucleotides, are organic molecules and named because they contain carbon and nitrogen. They are bases because they contain an amino group that has the potential of _________; thus, decreasing the hydrogen ion concentration in its environment and making it more basic.

A

binding an extra hydrogen

121
Q

Adenine and guanine are classified as______. The primary structure of a _______ is two carbon-nitrogen rings represented by adenine and guanine.

A

purines

122
Q

Cytosine, thymine, and uracil (RNA) on the other hand, are classified as _______ which have a single carbon-nitrogen ring as their primary structure

A

pyrimidines

123
Q

T or F. Purines have a double-ring structure, and
pyrimidines have a single ring.

A

T.

124
Q

The phosphate residue is attached to the hydroxyl group of the 5’carbon of one sugar and the hydroxyl group of the 3’carbon of the sugar of the next nucleotide, which forms a 5’-3’ ________

A

phosphodiester linkage.

125
Q

The two strands of the helix run in opposite directions,
meaning that the 5’ carbon end of one strand will face the 3’ carbon end of its matching strand. (This is referred to as ____________and is important to DNA replication and in many nucleic acid interactions.)

A

antiparallel orientation

126
Q

Only certain types of base pairing are allowed. For example, a certain purine can only pair with a certain pyrimidine. This means A can pair with T, and G can pair with C. This is known as the base complementary rule or __________

A

Chargaffs Rule.

127
Q

RNA, is mainly involved in the process of protein
synthesis under the direction of _____

A

DNA

128
Q

The mRNA is read in sets of three bases known as _______. Each ____ codes for a single amino acid. In this way, the mRNA is read and the protein
product is made. I

A

codons

129
Q

________ is one of the smallest of the four types of RNA, usually 70-90 nucleotides long. It carries the correct amino acid to the site of protein synthesis.

A

Transfer RNA (tRNA)

130
Q

_________ are the smallest RNA molecules, and their role involves the regulation of gene expression by interfering with the expression of certain mRNA messages.

A

MicroRNAs (miRNA)

131
Q

DNA dictates the structure of mRNA in a process known as _______n, and
RNA dictates the structure of a protein in a process called_______.

A

transcriptio; translation

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