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MicroBiology > Topic 2 Cell Chemistry > Flashcards

Topic 2 Cell Chemistry Flashcards

1
Q

What are Chemical Bonds?

A

electrostatic forces between positively charged protons of one atom and negatively charged electrons of another atom that hold these atoms together within a molecule or between molecules

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2
Q

What are intramolecular bonds? name some types of intramolecular bonds (4)

A
  • hold atoms in the same molecule together
  • Ionic bonds
  • Covalent bonds
  • Hydrogen bonds
  • Hydrophobic interactions
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3
Q

what are intermolecular bonds? name some types of intermolecular bonds (4)

A
  • form between two different molecules
  • Hydrogen bonds
  • Hydrophobic interactions
  • Electrostatic (ionic) forces
  • Van der Waals forces
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4
Q

why do bonds form?

A

bonds form between atoms to achieve a more stable situation

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5
Q

When are atoms the most stable? (2)

A
  1. ) Electrons in lowest possible energy levels
    2) Outermost energy level (valence shell or level) is filled to its maximum (2 or 8)

**To achieve this stability, most atoms most gain, lose or share electrons thus forming bonds and larger structures referred to as molecules

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6
Q

look at slides 5-10

A

all chemistry review :)

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7
Q

name the 5 compound types and state their charge/polarity, type of bonds, other info

A
  • Ionic – composed of all/mostly ionic bonds; generally water soluble to point of saturation (hydrophilic)
  • Polar – composed of all/mostly polar covalent bonds; generally water soluble (hydrophilic)
  • Nonpolar - composed of all/mostly non polar covalent bonds; not water soluble (hydrophobic)
  • Amphipathic – composed of part hydrophilic (ionic and/or polar) and part hydrophic (non polar) regions; on part water soluble, other part not
  • Solutions – solute and solvent
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8
Q

describe a hydrogen bond

A

“weak” bond that forms due to electrostatic interactions between hydrogen atoms (with positive polarity) and more electron-attracting (electronegative) atom (negative polarity)

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9
Q

Hydrogen has positive polarity because……

A

Hydrogen has positive polarity because it in polar covalent bond with larger, more electronegative atom (ie, oxygen or nitrogen)

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10
Q
  1. ) Multiple hydrogen bonds impart considerable (stability/instability) to molecules
  2. ) Plays (major/minor) role in the solubility and other properties of water
  3. ) Play (major/minor) roles in the biological properties of proteins
A
  1. ) stability
  2. ) major
  3. ) major
    * slides 13 and 14)
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11
Q

describe hydrophobic interactions

A

Weak bonds that occur when nonpolar molecules, or nonpolar regions of molecules, associate tightly in a polar solvent (ie, water); non polar molecules disrupt hydrogen bonding among water molecules so they “squeezed together or pushed” by water molecules to minimum their volume (therefore disrupting minimum number of hydrogen bonds)

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12
Q

why are hydrophobic interactions important? (3)

A

play important roles in…

  1. ) enzymes binding substrates
  2. ) protein conformation
  3. ) stabilization of RNA and cell membranes
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13
Q

what are van der waal forces?

A

weak attractive forces that occur between atoms when they become closer than 3–4 Å

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14
Q

van der waal forces occur due to…

A

temporary polarities in atoms and molecules

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15
Q

why are van der waal forces important?

A
  • Play important roles in enzymes binding substrates and protein–nucleic acid interactions
  • Play an important role in membrane fluidity
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16
Q

slides 18-20

A

Look at :)

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17
Q

what are monomers?

A

small molecules that are the building blocks of larger molecules

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18
Q

what are polymers?

A

larger molecules composed of covalently bonded similar or identical monomers

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19
Q

what are some inorganic molecules?

A

Water
Salts
Acids/Bases/Buffers

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20
Q

what are some organic molecules?

A 
Carbohydrates
Lipids
Polypeptide/Proteins
Nucleic Acids
Others
*slide 23
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21
Q

water is a polar molecule. this accounts for for of waters properties. name a few (4)

A

Can form hydrogen bonds and other bonds
Good solvent for polar and ionic molecules
High Specific heat
Exhibits cohesion and adhesion

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22
Q

describe salts

A

ionic compounds consisting of a cation and an anion held together by an ionic bond

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23
Q

Salts often ______ in water (a polar solvent) into their respective ____

A

dissociate; ions

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24
Q

describe acids

A

Proton donors; increase concentration of H+ ions in a solution

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25
describe bases
proton acceptors; decrease the concentration of H+ ions in a solution
26
describe buffers
compounds that resist changes in pH by sometimes behaving like an acid, and sometimes like a base; found in all cells
27
what are lipids? give examples and describe properties and function (4)
- fats, oils, sterols, other - Non Polar compounds - Hydrophobic - Play crucial roles in most membrane and as energy storage molecules
28
what are carbohydrates? give examples and describe what makes them up and a function
- monosaccharides,polysaccharides - Polymers of sugar units bonded together by glycosidic bonds - Play important roles in cell walls and as energy storage molecules
29
describe proteins and state what makes them up
- polymers of amino acids - Most abundant macromolecules in cells - Found throughout cell - Have important structural and enzymatic roles
30
what makes up nucleic acids? what are the two forms?
-polymers of nucleotides -Two forms (RNA and DNA) [RNA]>>>[DNA]
31
slide 29
just lots of shit- make sure to look at though!!
32
When other chemical species replace one or more of the hydroxyl groups on the sugar, _______ are formed
derivatives
33
slides 30-33
:)
34
what are the 4 polysaccharides? describe them
1. ) Disaccharides: carbohydrates containing two monosaccharides 2. ) Trisaccharides: carbohydrates containing three monosaccharides 3. ) Oligosaccharides: carbohydrates containing several monosaccharides 4. ) Polysaccharides: carbohydrates containing many monomeric units (monosaccharides) connected by glycosidic bonds
35
what are glycosidic bonds?
covalent bonds linking adjacent sugars together | **look at slide 35-36 for more information regarding this
36
what is starch? | what is its function?
- polysaccharide composed of glucose monomers joined to each other by alpha glycosidic bonds (tend to be hydrophobic) - Function is for energy storage
37
what are structural polysaccharides?
- (cellulose, chitin,etc) - polysaccharide composed of glucose monomers joined to each other by beta glycosidic bonds (hydrophobic) - Function is for structural strength of cell walls * slide 38
38
Polysaccharides can combine with other classes of | macromolecules to form complex polysaccharides. What are they? (2)
Glycoproteins - polysaccharides + proteins | Glycolipids - polysaccharides + lipids
39
what is the cellular function of glycoproteins?
Glycoprotiens include eukaryotic cell-surface receptor molecules; typically reside on external surfaces of the membrane
40
what is the cellular function of glycolipids?
Glycolipids important in cell walls of gram-negative bacteria
41
what are triglycerides composed of? what is its function? what type of bonds link everything together?
- Composed of three fatty acids bonded to the 3 carbon alcohol, glycerol - function is for energy storage - Has ester bonds (linkages) between glycerol and fatty acids
42
Fatty acids consist of _________ and __________
carboxyl group and hydrocarbon chain
43
what are saturated fatty acids?
no double bonds between Cs; straight, linear molecule
44
what are unsaturated fatty acids?
one or more double bonds between the carbons; bent or kinked molecule
45
what are complex lipids?
simple lipids that contain additional elements such as phosphorus, nitrogen, sulfur, or small hydrophilic organic compounds (e.g., sugars)
46
what are phospholipids?
complex lipids containing 2 fatty acids, glycerol, a phosphate group and something attached to phosphate (i,.e., ethanolamine)
47
why are phospholipids important?
play a major structural role in cytoplasmic membranes; amphipathic *slide 45 for picture
48
what is DNA? (3)
- polymer of deoxribonucleotides; genetic material in all cells and some viruses - Double-stranded in cells, complementary strands - Strands held together by hydrogen bonds
49
what is RNA? (3)
- RNA (ribonucleic acid) = polymer of ribonucleotides; plays role in protein synthesis in all cells; genetic material of most viruses - Typically single-stranded - Demonstrates secondary structure (folding back upon itself)
50
nucleotides are composed of... (3)
C5 sugar (pentose), either ribose (RNA) or deoxyribose (DNA) Nitrogen base Phosphate (nitrogen base attached to C5 sugar by N-glycosidic linkage and bonded to a phosphate)
51
why are nucleotides important? (4)
- Major components of nucleic acids - Key forms of chemical energy (e.g., ATP) - Carriers of sugars in biosynthesis of polysaccharides - Regulatory molecules for certain enzymes or metabolic events * slide 49
52
Nitrogen bases of nucleic acids belong to two chemical classes. What are they and what do they consist of?
1. ) Purine bases (adenine and guanine): contain two fused heterocyclic rings 2. ) Pyrimidine bases (thymine, cytosine, and uracil): contain a single six-membered heterocyclic ring
53
slides 51-55
:) | **MAKE SURE to read slide 53; did not make into card
54
what are for 4 classes RNA?
mRNAs, tRNAs, rRNAs, and small RNAs
55
what are enzymes?
catalytic proteins; catalysts for chemical reactions
56
what are structural proteins?
Integral parts of cellular structures (such as eukaryotic chromosomes)
57
most amino acids consist of _____________________ 2 of 22 contain _____, 1 contains _______
-carbon, hydrogen, oxygen, and nitrogen; sulfur;selenium
58
amino acids contain 2 important functional groups. what are they?
Carboxylic acid group (-COOH) Amino group (-NH2) *slide 59
59
Adjacent amino acid monomers held together by covalent bonds called _______
peptide bond
60
slides 60-64
:)
61
what are isomers?
related, but nonidentical molecules
62
what are optical isomers?
enantiomers (sterioisomers or mirror image isomer); have same chemical properties but often have different physical properties *slide 66-68
63
what are racemasses?
enzymes capable of interconverting specific enantiomers
64
what is a polypeptide?
structural term meaning a series of amino acids (10s,100s,1000s or 10,000s amino acids long) joined to each other by peptide bonds
65
Each polypeptide has an ______ end and a _____ end
amino; carboxyl
66
what is a protein?
a functional unit consisting of one or more polypeptides having one or more functions.
67
what is primary structure in relation to proteins/polypeptide
linear array of amino acids in a polypeptide
68
what is secondary structure in relation to proteins/polypeptide
localized folds or twists in parts of polypeptide that form a more stable structure; held together by hydrogen bonding between amino group Hydrogen and carbonyl Oxygen *slides 71 and 72
69
Tertiary structure of a protein? | what does it form and why is this important?
- overall, 3 dimensional shape of a polypeptide - Forms exposed regions or grooves in the molecule (i.e., active site) - important for binding to other molecules * slide 74
70
tertiary structure is held together by... (4)
Held together by 1) hydrogen bones, 2) electrostatic interactions, 3) hyrophobic interactions with water and 4) Disulfide bonds: covalent bonds between -SH groups from two different amino acids *slide 74
71
what is the Quaternary structure of a protein?
overall arrangement of polypeptides in a protein; only found in proteins composed of two or more polypeptides *slide 75-77
72
what is denaturation?
Unfolding of Polypeptide Chains
73
what can cause denaturation?
Extremes of pH High temperatures Certain chemicals
74
what does denaturation result in?
Causes loss of biological function
75
is denaturation reversible?
Can be reversible or irreversible

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