Chapter 5 Flashcards

1
Q

Macromolecules

A

Carbohydrates
Lipids
Proteins
Nucleus acids

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2
Q

Polymer

A

Is a long molecule consisting of many similar or identical building blocks linked by covalent bonds.

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3
Q

Monomers

A

Are the repeating units that serve as the building blocks of a polymer. (Are smaller molecules)

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4
Q

Chain-like macromolecules

A

Carbohydrates
Proteins
Nucleic Acid

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5
Q

Enzymes

A

Specialized macromolecules that speed up chemical reactions.

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6
Q

Dehydration reaction

A

A reaction in which two molecules are covalently bonded to each other, with the loss of a water molecule. This is how monomers are connected to each other.

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7
Q

Hydrolysis

A

The bond between monomers is broken by the addition of a water molecule, with a hydrogen from water attaching to one monomer and the hydroxyl group attaching to the other.

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8
Q

Carbohydrates

A

Include sugars and polymers of sugars.
Monosaccharides, disaccharides, and polysaccharides.

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9
Q

Monosaccharides’ general molecular formula

A

CH2O

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10
Q

Glucose structure

A

C6H12O6. Has a carbonyl group and multiple hydroxyl groups. Is an aldose (aldehyde sugar). Forms rings.

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11
Q

Most common monosaccharide

A

Glucose

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12
Q

Carbohydrate carbon skeleton size

A

Three to seven carbons long

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13
Q

Trioses

A

Three-carbon sugars.

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14
Q

Pentoses

A

Five-carbon sugars. Form rings.

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15
Q

Asymmetric carbon

A

A carbon attached to four different atoms or groups of atoms.

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16
Q

Glycosidic linkage

A

A covalent bond formed between two monosaccharides by a dehydration reaction.

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17
Q

Maltose

A

Disaccharide formed by two molecules of glucose. Present in beer.

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18
Q

Sucrose

A

Disaccharide made of glucose and fructose. Known as table sugar.

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19
Q

Lactose

A

Disaccharide made of glucose and galactose. Present in milk.

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20
Q

Polysaccharides

A

Are macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages.

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21
Q

Architecture and function of a polysaccharide is determined by…

A

It’s sugar monomers and the position of its glycosidic linkages.

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22
Q

Starch

A

Plants use starch to store excess glucose. Starch represents stored energy.

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23
Q

Glycogen

A

A polymer of glucose that is like amylopectin (complex starch) but more extensively branched. Animals use glycogen to store sugar mainly in muscle and liver cells.

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24
Q

Cellulose

A

Polysaccharide present in cell walls. The most abundant organic compound on Earth.

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25
Two rings that form glucose
Alpha and beta
26
Chitin
Carbohydrate used by arthropods to build their exoskeletons.
27
Lipids
They mix poorly, if at all, with water. Generally not big enough to be considered macromolecules.
28
Lipids consist of mostly…
Hydrocarbon regions.
29
Lipids most biologically important molecules
Fats, phospholipids, and steroids
30
Fats
A fat is constructed from glycerol and fatty acids.
31
Glycerol
Is an alcohol. (Each of its 3 carbons carries a hydroxyl group)
32
Fatty acid
A fatty acid has a long carbon skeleton, usually 16 or 18 carbon atoms in length. The carbon at one end is part of a Carboxyl group (acid). The rest of the skeleton is a hydrocarbon chain (hydrophobic).
33
Triacylglycerol
Three fatty acid molecules are each joined to glycerol by an ester linkage, a bond formed via dehydration reaction between a hydroxyl group and a carboxyl group.
34
Saturated fatty acid
Has a carbon skeleton without double bonds, only single bonds.
35
Unsaturated fatty acid
Has one or more double bonds. Nearly all of these double bonds are cis double bonds.
36
Saturated fats are solid at room temperature
True
37
Unsaturated fats are liquid at room temperature
True
38
Trans fats
Have trans double bonds resulting from hydrogenating unsaturated fats.
39
Major Function of fats
Energy Storage
40
A gram of fat stores more than twice as much energy as a gram of polysaccharide
True
41
Phospholipid
Has only two fatty acids attached to glycerol. The third hydroxyl group of glycerol is joined to a phosphate group, which has a negative charge.
42
A phospholipid’s phosphate group and its attachments form a…
Hydrophilic head
43
When phospholipids are added to water
They for a bilayer, shielding their hydrophobic tail from water.
44
Steroids
Are lipids characterized by a carbon skeleton consisting of four fused rings.
45
Cholesterol
A type of steroid. It is a common component in animal cell membranes and is the precursor form from which other steroids are synthesized.
46
Proteins account for more than 50% of the dry mass of most cells, and they are instrumental in almost everything organisms do.
True
47
Different protein functions
Speed up chemical reactions Defense Storage Transport Cellular communication Movement Structural support
48
Catalysts
Chemical agents that selectively speed up chemical reactions without being consumed by the reaction.
49
Proteins are the most structurally sophisticated molecules known
True
50
Proteins are constructed from a set of…
20 amino acids
51
Peptide bond
The bond between amino acids
52
Polypeptide
Polymer of amino acids linked by peptide bonds.
53
Protein
Is a biologically functional molecule made up of one or more polypeptides, each folded and coiled into a specific three-dimensional structure.
54
Amino acid
Is an organic molecule with both an amino group and a carboxyl group.
55
The R group (the side chain)
A variable group that differs with each amino acid. Determines the unique characteristics of a particular amino acid.
56
How do the amino groups and carboxyl groups usually exist at the pH found in a cell?
In ionized form.
57
Groups of amino acids acids according to the properties of their side chains (R groups)
Nonpolar side chains; hydrophobic Polar side chains; hydrophilic Electrically charged side chains; hydrophilic
58
How does a Peptide bond occur?
Results from two adjacent amino acids; where the carboxyl group of one amino acid is next to the amino group of the other, here they can become joined via dehydration reaction resulting in a peptide bond.
59
Polypeptide backbone
The amino acids in a polypeptide with the exception of the R groups.
60
Single amino end in a polypeptide
N-terminus
61
Single carboxyl end in a polypeptide
C-terminus
62
The chemical nature of a polypeptide is determined by…
The kind and sequence of the side chains.
63
Globular proteins
Roughly spherical proteins
64
Fibrous proteins
Proteins that are shaped like long fibers.
65
The function of a protein depends on…
It’s ability to recognize and bind to some other molecule.
66
All proteins share ___ levels of superimposed structure.
Three; primary, secondary, and tertiary structure.
67
Primary structure
The primary structure of a protein is its sequence of amino acids, which is determined by inherited genetic information.
68
Secondary structure
The coils and folds in a polypeptide.
69
How is the secondary structure of a protein (the coils and folds) sustained?
The coils and folds are the result of hydrogen bonds between the repeating constituents of the polypeptide backbone. Within the backbone, the oxygen atoms have a partial negative charge, and the hydrogen atoms attached to the nitrogens have a partial positive charge; therefore, hydrogen bonds can form between these atoms.
70
α (Alpha) helix
A delicate coil held together by hydrogen bonding between every fourth amino acid.
71
β pleated sheet
Two or more segments of β strands that are connected by hydrogen bonds.
72
β strand
The polypeptide chain lying side by side.
73
Tertiary structure
Is the overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids.
74
Hydrophobic interaction
A type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water. This contributes to tertiary structure.
75
What holds close non polar amino acid side chains together?
van der Waals interactions
76
Disulfide bridges
Covalent bonds where two cysteine monomers, which have Sulfhydryl groups (—SH) on their side chains, are brought close together by the folding of the protein. The sulfers bond and form the disulfide bridge (—S—S—). This bridge rivets parts of the protein together.
77
Quaternary structure
Is the overall protein structure that results from the aggregation of it’s polypeptide subunits. These proteins must consist of two or more polypeptide chains.
78
Collagen account for __% of the protein in a human body.
40%
79
Examples of proteins with quaternary structure
Fibrous protein : Collagen Globular protein : Hemoglobin
80
Sickle-cell disease
An inherited blood disorder that is caused by the substitution of valine (amino acid) for glutamic acid (amino acid) at a particular position in the primary structure of hemoglobin.
81
Denaturation
A change caused by the wrong pH, salt concentration, temperature, or other aspects of the environment that destroys the weak bonds and interaction within a protein, which causes the protein to unravel and lose its native shape.
82
A denatured protein is…
Biologically inactive
83
Denaturing agents include:
Chemicals that disrupt the hydrogen bonds, ionic bonds, and disulfide bridges of a protein.
84
The information for building specific shape is intrinsic to the protein’s ____________
Primary structure
85
Chaperonins (chaperone proteins)
Protein molecules that assist in the proper folding of other proteins.
86
Diseases caused by misfolding of polypeptides:
Cystic fibrosis, Alzheimer’s, Parkinson’s, and mad cow disease.
87
X-ray Cristallography
Technique used to determine the 3D structure of proteins.
88
Nuclear Magnetic Resonance Spectroscopy (NMR)
Another method for analyzing protein structure which does not require protein crystallization.
89
Bioinformatics
Can be used to predict protein structure and function.
90
Nucleic acids
Are polymers made of monomers called nucleotides.
91
Two types of Nucleic acid
Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA)
92
Process of gene expression
- DNA provides information for its own replication - DNA directs RNA synthesis and controls protein synthesis
93
Each chromosome contains _____________ which carries several hundred or more _____
One long DNA molecule Genes
94
Proteins are required to _________
Implement genetic programs
95
messenger RNA (mRNA)
mRNA interacts with ribosomes to direct production of a polypeptide.
96
Polynucleotide
Polymer of Nucleic acid
97
Nucleotide
Three parts: Five-carbon sugar (pentose) Nitrogen-containing (nitrogenous) base One or more phosphate groups
98
In a polynucleotide, each monomer has only ________________
One phosphate group
99
Nucleoside
The portion of a nucleotide without any phosphate groups.
100
Each nitrogen base has…
One or two rings that include nitrogen atoms.
101
Why are they called nitrogen ‘bases’?
Because the nitrogen atoms tend to take up H+ from solution, thus acting as bases.
102
Two families of nitrogenous bases
Pyrimidines Purines
103
Pyrimidine
Has one six-membered ring of carbon and nitrogen atoms.
104
Members of the pyrimidine family
Cytosine (C) Thymine (T) Uracil (U)
105
Purines
Are larger, with a six-membered ring fused to a five-membered ring.
106
Members of the purine family
Adenine (A) Guanine (G)
107
Thymine is found only in ____
DNA
108
Uracil is only found in ____
RNA
109
Deoxyribose
DNA sugar
110
Ribose
RNA sugar
111
Difference between deoxyribose and ribose
Deoxyribose lacks an oxygen atom on the second carbon in the ring.
112
Nucleoside monophosphate
Nucleotide
113
Phosphodiester linkage
Bond which joins adjacent nucleotides.
114
Sugar-phosphate backbone
Sugar, phosphate group, and phosphodiester linkages.
115
Two free ends of polynucleotide
One end has a phosphate attached to a 5’ carbon And the other end has a hydroxyl group on a 3’ carbon.
116
Genes are ______ of nucleotides long
Hundreds to thousands
117
Double helix of DNA is formed by…
Two polynucleotides that wind around an imaginary axis; they are antiparallel and are held together by hydrogen bonds between the bases.
118
Adenine pairs with…
Thymine
119
Guanine pairs with…
Cytosine
120
Thymine pairs with…
Adenine
121
Cytosine pairs with…
Guanine
122
RNA molecules exist as single strands.
True
123
The functional shape of RNA results from
Base pairing.
124
In RNA, adenine pairs with…
Uracil