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Microbiology > Cell Chemistry Review > Flashcards

Cell Chemistry Review Flashcards

1
Q

hold atoms in the same molecule (include ionic bonds, covalent bonds, hydrogen bonds, hydrophobic interactions)

A

intramolecular bonds

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2
Q

form between two different molecules (include hydrogen bonds, hydrophobic interactions, electrostatic forces, Van Der Waals forces)

A

intermolecular bonds

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3
Q

formed by attraction of oppositely charged ions, fill valence shell, dissociate in presence of water

A

ionic bond

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4
Q

strong bond between chemical elements where electrons are shared between atoms to fill valence shells, can have double and triple bonds

A

covalent bond

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5
Q

types of covalent bonds

A

electronegativity, non-polar, polar

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6
Q

the force of attraction of a nucleus on the electrons moving around it

A

electronegativity

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7
Q

electrons are shared equally and there is no polarity, occurs between atoms of similar electronegativity

A

non-polar bond

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8
Q

electrons are shared unequally between two atoms so there is a positive and negative pole (zero net charge), occurs with atoms of varying electronegative values

A

polar bond

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9
Q

Why is polarity important?

A

water is a polar solvent, macromolecules are polar and readily dissolve in water, promotes molecular stability through hydrogen bonds

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10
Q

composed of mostly ionic bonds, generally water soluable, hydrophilic

A

ionic compounds

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11
Q

mostly polar covalent bonds, generally water soluable, hydrophilic

A

polar compounds

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12
Q

mostly non polar covalent bonds, not water soluble (hydrophobic)

A

nonpolar compounds

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13
Q

composed of part hydrophilic and hydrophobic regions, part water soluable while other parts not

A

amphipathic compound

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14
Q

What makes up a solution?

A

a solute and a solvent

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15
Q

small molecules that are the building blocks of larger molecules

A

monomers

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16
Q

large molecules

A

macromolecules

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17
Q

larger molecules composed of covalently bonded similar or identical monomers

A

polymers

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18
Q

a weak bond that forms due to electrostatic interactions between hydrogen atoms (positive polarity) and more electron-attracting atoms (negative charge)

A

hydrogen bond

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19
Q

weak bonds that occur when nonpolar molecules or regions associate tightly in a polar solvent, nonpolar molecules disrupt hydrogen bonding among water molecules, squeeze together by water molecules trying to minimize volume

A

hydrophobic interactions

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20
Q

weak attractive forces that occur between atoms when they are nearly touching, due to temporary polarities in atoms and molecules

A

Van der Waals forces

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21
Q

__________is a component of all macromolecules

A

carbon

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22
Q

functional group that can act as an acid, makes the molecule more polar

A

carboxyl group

OH-C=O

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23
Q

makes molecule an alcohol and more polar

A

hydroxyl group

-C-OH

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24
Q

makes molecule an organic base and more polar

A

amino group

-N-HH

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25
carbon oxygen carbon with a double bonded oxgygen on the first carbon
ester
26
carbon oxygen carbon with 2 hydrogens on both carbons
ether
27
water, salts, acids, bases, and buffers
inorganic molecules
28
carbohydrates, lipids, polypeptides, and proteins
organic molecules
29
makes up 90% of a cell, has a high specific heat, good solvent for polar and ionic molecules, can form hydrogen bonds, key features are polarity and cohesion
water
30
importance of cohesion
water molecules have a high affinity for one another due to hydrogen bonds between, allows for high surface tension and specific heat
31
ionic compounds consisting of a cation and an anion held together by and ionic bond, dissolve in water into there respective ions
salts
32
proton donors, increases the concentration of H+ ions in solutions
acids
33
proton acceptors, decrease the concentration of H+ ions in a solution
bases
34
compounds that resist changes in pH by sometimes behaving like an acid or a base
buffer
35
What are the 4 kinds of macromolecules?
proteins, nucleic acids, lipids, carbohydrates
36
organic compounds, C1H2O1, polar and hydrophilic, 4-7 carbon atoms, used for energy storage and polysaccharide building blocks
monosaccharides and disaccharides
37
carbohydrates with many monomeric units connected by glycosidic bonds
polysaccharides
38
carbohydrates containing 2 monosaccharides
disaccharide
39
carbohydrates containing 3 monosaccharides
trisaccharides
40
carbohydrates containing several monosaccharides
oligosaccharides
41
covalent bonds linking sugars together in a polysaccharide, alpha and beta linkage
glycosidic bond
42
polysaccharide composed of glucose monomers, joined to each other by alpha glycosidic bond, function is for energy storage
starch
43
examples include cellulose and chitin, polysaccharide composed of glucose monomers joined to each other by beta glycosidic bonds
structural polysaccharide
44
polysaccharide + protein
glycoproteins
45
polysaccharide + lipid
glycolipid
46
include simple fats, oils, sterols, and phospholipids, both nonpolar and hydrophobic, fatty acids are major constituents
lipids
47
3 fatty acids bound to the C3 alcohol glycerol, used for energy storage, also known as triglycerides
simple lipids
48
a lipid characteristic with no double bond, linear
saturated
49
a lipid characteristic with one or more double bonds between the carbohydrates
unsaturated
50
quality that means both hydrophilic and hydrophobic characteristics are displayed
amphipathic
51
simple lipids that contain additional elements or small hydrophilic compounds
complex lipids
52
complex lipids containing PO4 groups, seen in membranes and are amphipathic
phospholipids
53
made up of a polymer of nucleotides
nucleic acids
54
a polymer of deoxiribonucleotides, genetic material in all cells and some viruses, double strand, complementary strands, Hydrogen bond connection
DNA
55
polymer of ribonucleotides, plays role in protein synthesis, genetic material of most viruses, composed of one C5 sugar, nitrogen base, and phosphate group, typically a single strand, exhibits secondary structure (folds over), has four classes
RNA
56
nitrogen base bonded to C5 sugar
nucleoside
57
nitrogen base attached to C5 sugar by N-glycosidic linkage, are a major component of nucleic acids, key forms of chemical energy
nucleotide
58
adenine and guanine, contain 2 fused heterocyclic rings
purine bases
59
cytosine, thymine, and uracil, contain a 6 membraned heerocyclic ring
pyrimidine bases
60
phosphate linkage that connects 2 sugars with ester linkage
phosphodiester bond
61
sequence of nucelotides in RNA/DNA molecule
primary structure
62
What are the 4 classes of RNA?
mRNA, tRNA, rRNA, and small RNA
63
A peptide bond releases ___________
water
64
a macromolecule that mostly consists of carbon, hydrogen, oxygen, and nitrogen, contain 2 important functional groups (amino group and carboxylic group)
amino acids
65
related, but not completely identical, include optical isomers known as enantiomers or sterioisomers
isomers
66
enzymes capable of interconverting specific enantiomers
racemases
67
structural term meaning a series of amino acids (10s, 100s, 1000s, 10,000s amino acids longs) joined to each other by peptide bonds
polypeptide
68
a functional unit consisting of one or more polypeptide having one or more functions
protein
69
catalytic proteins, catalysts for chemical reactions
enzymes
70
integral parts of cellular structures (such as eukaryotic chromosomes)
structural proteins
71
two amino acids bonded by peptide linkage
dipeptide
72
three amino acids bonded by peptide linkage
tripeptide
73
many amino acids bonded by peptide linkage
polypeptide
74
linear array of amino acids in a polypeptide
primary structure
75
folds in polypeptide that form a more stable structure, held together by hydrogen bonding between amino group hydrogen and carbonyl oxygen
secondary structure
76
additional folding of polypeptide to result in greater stability and unique three dimensional shape, forms exposed regions or grooves in the molecule that are important for binding other molecules
tertiary structure
77
covalent bonds between -SH group from two different amino acids
disulfide bond
78
occurs in proteins composed of two or more polypeptides
quaternary structure
79
each polypeptide in the protein, held together by covalent or noncovalent linkages
subunit
80
protein containing two identical subunits
homodimer
81
protein containing two nonidentical subunits
heterodimer
82
What factors can lead to the denaturation of polypeptide chains?
extreme change in pH value, temperature or exposure to chemicals. results in loss of biological function and can be reversible or irreversible

Microbiology (11 decks)

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