1
Q
Most diverse macromolecules
A
Proteins
2
Q
Made up of amino acids
A
Proteins
3
Q
Helps different cells to keep in shape
A
Proteins
4
Q
Structure of amino acids
A
Amino group
Carboxyl group
R-group or side chain
5
Q
Acidic group in the structure of amino acids
A
Carboxyl group
6
Q
Basic group in structure of amino acids
A
Amino group
7
Q
This varies for every amino acid
A
R-group or side chain
8
Q
All amino acids have a high melting point greater than __
A
200C
9
Q
Amino acids are soluble in __, slightly soluble in __, and dissolve with difficulty in __
A
Water
Alcohol
Methanol, ethanol, and propanol
10
Q
In amino acids, these play an important role in solubility
A
R-group of amino acids and pH of the solvent
11
Q
On heating to high temperature, amino acids __
A
Decompose
12
Q
All amino acids (except __) are __
A
Glycine
Optically active
13
Q
Amino acids can connect with a peptide bond involving their __
A
Amino and carboxyl group
14
Q
A covalent bond formed between the alpha-amino group of one amino acid and an alpha-carboxyl group of other forming __
A
-CO-NH-linkage
15
Q
Are planar and partially ionic
A
Peptide bonds
16
Q
Is a molecule with functional groups, of which at least one has a positive and one has negative electrical charge
A
Zwitterion/zwitterionic property
17
Q
In nature, amino acids act as both acids and base due to the two amine and carboxyl groups present
A
Amphoteric property
18
Q
Detects presence of a-amino acids
A
Ninhydrin test
19
Q
Detects the presence of amino acid chain
A
Xanthoproteic test
20
Q
Detects free amino group in the peptide chain
A
Reaction with Sanger’s reagent
21
Q
Detects presence of amino acid group
A
Reaction with nitrous acid
22
Q
Classification of amino acids:
A
Non-polar, aliphatic R-group
Polar, uncharged R-group
Positively charged R-group
Negatively charged R-groups
Non-polar, aromatic R-groups
23
Q
Non-polar, aliphatic r-group
A
Glycine
Alanine
Valine
Leucine
Methionine
Isoleucine
24
Q
Polar, uncharged r-group
A
Serine
Threonine
Cysteine
Proline
Asparagine
Glutamine
25
Positively charged r-group
Lysine
Arginine
Histidine
26
Negatively charged r-groups
Aspartate
Glutamate
27
Non-polar, aromatic r-groups
Phenylalanine
Tyrosine
Tryptophan
28
Enantiomeric molecules have an optical property known as __
Optical activity
29
The ability to rotate the plane of plane-polarized light.
Optical activity
30
Clockwise rotation (optical activity)
Dextrorotatory behavior
31
Counterclockwise rotation (optical activity)
Levorotatory behavior
32
A relative ranking of the “priority” of various functional groups is given as
SH>OH>NH2>COOH>CH2OH>CH3>H
33
A chiral center has __ different functional groups
Four
34
If the priorities of functional groups with a chiral center goes in a clockwise rotation
R chirality
35
If the priorities of functional groups with a chiral center goes in a counterclockwise rotation
S chirality
36
This is a function of all ionizable groups on the amino acid, including the amino and carboxyl functional groups in addition to any ionizable group on the side chain.
Isoelectric point
37
pH at which the amino acid has a neutral charge
Isoelectric point
38
In order to determine the nature of the molecular and ionic species that are present in aqueous solutions at different pH’s, we make use of the __
Henderson-Hasselbalch Equation
39
Henderson-Hasselbalch equation:
pKa = pH + log10 (HA/A-)
40
Represents the acidity of a specific conjugate acid function (HA)
pKa
41
When the pH of the solution equals pKa, the concentrations of HA and A- must be __
Equal
42
At neutral pH the amino group is __, and the carboxyl group is __
Protonated
Deprotonated
43
You could show that the amino acid now existed as a negative ion using
Electrophoresis
44
The reaction is simply the transfer of the -H from the acid to the amine and the attraction of the positive and negative charges
Salt formation reaction
45
In salt formation reaction, the acid group becomes __, and the amine nitrogen becomes __ because of the positive hydrogen ion
Negative
Positive
46
This amino acid undergoes oxidation and reduction reactions involving the -SH (sulfhydryl group)
Cysteine
47
The oxidation of two sulfhydryl groups results in the formation of a __ by the removal of two hydrogens
Disulfide bond
48
Combination of amino acids in which the amine group of one amino acid has undergone a reaction with the carboxyl group of another amino acid
Condensation reaction
49
The amide bond that occurs between the amine nitrogen of one amino acid and the carboxyl carbon of another amino acid
Peptide bond
50
Level of protein structure
Primary structure
Secondary structure
Tertiary structure
Quarternary structure
51
Is the amino acid sequence of the protein
Primary structure
52
Is unique and defines the function of the protein
Amino acid sequence (primary structure)
53
Highly regular sub-structure of the protein
Secondary structure
54
The two most common types of protein secondary structures are the __
Alpha helix and the beta-sheet
55
Overall three-dimensional structure of the protein
Tertiary structure
56
Typical protein consists of several sections of a specific secondary structure (alpha helix or beta-sheet) along with other areas in which a more random structure occurs
Tertiary structure
57
Refers to the specific interaction and orientation of the subunits of that protein
Quarternary structure
58
Protein that is more soluble in water
Globular protein
59
Protein that is insoluble in water
Fibrous protein
60
Proteins that function to help cells keep their shape
Structural proteins
61
Proteins that make up muscle tissues
Connective and motor proteins
62
Proteins that transport items in and out of cells
Transport proteins
63
Are proteins that speed up chemical reactions in cells
Enzymes
64
Proteins that bund to foreign substances such as bacteria and target them for destruction
Antibodies
65
Human red blood cells contain a protein called __, which binds with oxygen
Hemoglobin
66
Allows the blood to carry oxygen from the lungs to cells throughout the body
Hemoglobin
67
Supplies kinetic energy to protein molecules, causing their atoms to vibrate more rapidly and disrupting relatively weak hydrogen bonding and dispersion forces
Heat about 50C or ultraviolet (UV) radiation
68
These compounds ate capable of engaging in intermolecular hydrogen bonding with protein molecules, disrupting intramolecular hydrogen bonding within the protein
Use of organic compounds, such as ethyl alcohol
69
These ions form strong bonds with the carboxylate anions of the acidic amino acids or SH groups of cysteine, disrupting ionic bonds and disulfide linkages
Salts of heavy metal ions, such as mercury, silver, and lead
70
71
These reagents combine with positively charged amino groups in proteins to disrupt ionic bonds
Alkaloid reagents, such as tannic acid (used in tanning leather)
72
are in the form of tertiary and quarternary structure
Enzyme
73
acts as a catalyst in cellular reactions
Enzyme
74
are reusable
Enzyme
75
Lower the activation energy (or energy needed to start a reaction), and cause the reaction to occur more quickly
Catalysts
76
Biological catalysts are called
Enzymes
77
Globular proteins usually found in nuclear region of cells
Enzyme
78
Catalyze the splitting of RNA; breaks down or synthesize complex molecules (lower Ea)
Enzyme
79
Each enzyme has a __
Specific substrate
80
Classification of enzymes:
Oxidoreductases
Transferases
Hydrolases
Isomerases
Lyases
Ligases
81
Catalyzes the oxidation reaction where electrons tend to travel from one form of a molecule to the other
Oxidoreductase
82
Help in the transportation of the functional group among acceptors and donor molecules
Transferases
83
Are hydrolytic enzymes, which catalyze hydrolysis reaction by adding water to cleave the bind and hydrolyze it
Hydrolases
84
Catalyze the structural shifts present in a molecule, thus causing change in the shape of the molecule
Isomerases
85
Adds water, carbon dioxide, or ammonia across double bonds or eliminate these to create double bonds
Lyases
86
These catalyze the breakage of bonds without catalysis
Lyases
87
Are known to charge the catalysis of a ligation process
Ligases
88
Each enzyme has a unique shape, including the groove called __
Active site
89
How does enzyme works?
Specific substrate binds to active site causing substrate to become unstable and react resulting to a product to be released from the active site
90
When an enzyme is interacting with its substrate during chemical reaction, together they ate referred to as __
Enzyme-subtrate complex
91
Factors affecting enzyme activity:
Concentration of substrate and enzyme
Temperature
Hydrogen ion concentration (pH)
Inhibitors
92
Temperature above normal range __ enzymes
Denature
93
Most enzymes work best at what pH level
near neutral (pH 6 to 8)
94
As the concentration of the substrate increases, __ until it achieves its saturation point
So does the rate of enzyme activity
95
When the concentration of substrate increases, the rate of reaction __
Increases
96
When the concentration of the enzyme increases, the rate of reaction __
Increases
97
Once all the enzyme molecules are saturated with substrate, an increasing in the concentration of either one will __
Not alter the rate of reaction
98
Two types of enzyme inhibitors
1. Competitive inhibitor
2. Non-competitive inhibitor
99
Chemical that resemble the enzyme’s normal substrate and compete with it for the active site
Competitive inhibitor
100
Does not enter the active site, but bind to another part of the enzyme, causing the enzyme and active site to change the shape
Non-competitive inhibitor
101
Enzyme regulation:
1. Genetic control of enzyme synthesis through repression, induction, or enhancement of transcription
2. Genetic control of enzyme synthesis through promoter recognition and through DNA supercoiling
3. Genetic control of enzyme synthesis through the translational control of enzyme synthesis
4. Controlling of the enzyme’s activity (feedback inhibition)
102
Are molecules that store information for cellular growth and reproduction
Nucleic acids
103
Nucleic acids are:
Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA)
104
Nucleic acids are large molecules consisting of long chains of monomers called
Nucleotides
105
Nucleic acids are comprised of nucleotides that consist of:
Base with nitrogen
Pentose sugar
Phosphoryl group
106
The bases in DNA and RNA are:
Pyrimidines C, T, and U
Purines A and G
107
The pentose sugar in RNA
Ribose
108
The pentose sugar in DNA
Deoxyribose
109
Has a base linked by a glycosidic bond to C1’ of a sugar (ribose or deoxyribose)
Nucleoside
110
A nucleoside is named by changing the end of the base name to __for purines and __ for pyrimidines
-osine
-idine
111
Has a phosphoryl group attached to the C5’—OH group of a nucleoside
Nucleotide
112
Forms when the —OH on C5’ of a sugar in a nucleoside bonds to hydrogen phosphate
Nucleotide
113
This rule states that the % of adenine is the same as the % of thymine; and the % of guanine is the same as the % of cytosine
Chargaff’s rule
114
Adenine is always linked by __ to thymine
two hydrogen bonds
115
Guanine is always linked by __ to cytosine
three hydrogen bonds
116
Is a sequence of nitrogenous bases in an mRNA that determines the amino acid order for the protein
Genetic code
117
The genetic code consists of sets of three bases (triplets) along the mRNA called __
Codons
118
Transmits information from DNA to make proteins
RNA
119
Several types of RNA:
Messenger RNA (mRNA)
Transfer RNA (tRNA)
Ribosomal RNA (rRNA)
120
Carries genetic information from DNA to the ribosomes
mRNA
121
Brings amino acids to the ribosome to make the protein
tRNA
122
Makes up 2/3 of ribosomes where protein synthesis takes place
rRNA
123
In humans, the % of total rRNA is
80%
124
In humans, the % of total mRNA is
5%
125
In humans, the % of total tRNA is
15%
126
Major component of the ribosomes
rRNA (80%)
127
Protein synthesis involves:
Transcription
Translation
128
In which mRNA is formed from a gene on a DNA strand
Transcription
129
In which tRNA molecules bring amino acids to mRNA to build a protein
Translation
130
In transcription one strand of DNA is copied, starting at the initiation point which has the sequence __
TATAAA
131
During transcription, __ moves along the DNA template in the 3’-5’ direction to synthesize the corresponding mRNA
RNA Polymerase
132
DNA contains __ that code for proteins
Exons
133
DNA contains __ that do not code for proteins
Introns
134
Regulation of transcription in which the end products speed up or slow the synthesis of mRNA
Feedback control
135
Regulation of transcription un which high levels of a reactant induced the transcription process to provide the necessary enzymes for that reactant
Enzyme induction
136
Alters the nucleotide sequence in DNA; results from mutagens such as radiation and chemicals
Mutation
137
Produces one or more incorrect codons un the corresponding mRNA; produces a protein that incorporates one or more incorrect amino acid
Mutation
138
Causes genetic diseases that produce defective proteins and enzymes
Mutation
139
In this, a different base substitutes for the proper base in DNA
Substitution mutation
140
In this, there is a change in a codon in the mRNA; the wrong amino acid may be placed in the polypeptide
Substitution mutation
141
In this, an extra base adds to or is deleted from the normal DNA sequence
Frame shift mutation
142
In this, the codons in mRNA and the amino acids are incorrect from the base change
Frame shift mutation
143
Genetic diseases:
Galactosemia
Cystic fibrosis
Down syndrome
Familial hypercholesterolemia
Muscular dystrophy
Huntington’s disease
Sickle-cell anemia
Hemophilia
Tay-Sachs disease
2C
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