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MicroBiology > Topic 2 Cell Chemistry > Flashcards

Topic 2 Cell Chemistry Flashcards

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Biology 101 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
Q

describe bases

A

proton acceptors; decrease the concentration of H+ ions in a solution

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26
Q

describe buffers

A

compounds that resist changes in pH by sometimes behaving like an acid, and sometimes like a base; found in all cells

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27
Q

what are lipids? give examples and describe properties and function (4)

A
  • fats, oils, sterols, other
  • Non Polar compounds
  • Hydrophobic
  • Play crucial roles in most membrane and as energy storage molecules
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28
Q

what are carbohydrates? give examples and describe what makes them up and a function

A
  • monosaccharides,polysaccharides
  • Polymers of sugar units bonded together by glycosidic bonds
  • Play important roles in cell walls and as energy storage molecules
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29
Q

describe proteins and state what makes them up

A
  • polymers of amino acids
  • Most abundant macromolecules in cells
  • Found throughout cell
  • Have important structural and enzymatic roles
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30
Q

what makes up nucleic acids? what are the two forms?

A

-polymers of nucleotides
-Two forms (RNA and DNA)
[RNA]»>[DNA]

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31
Q

slide 29

A

just lots of shit- make sure to look at though!!

32
Q

When other chemical species replace one or more of the hydroxyl groups on the sugar, _______ are formed

A

derivatives

33
Q

slides 30-33

A

:)

34
Q

what are the 4 polysaccharides? describe them

A
  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
Q

what are glycosidic bonds?

A

covalent bonds linking adjacent sugars together

**look at slide 35-36 for more information regarding this

36
Q

what is starch?

what is its function?

A
  • polysaccharide composed of glucose monomers joined to each other by alpha glycosidic bonds (tend to be hydrophobic)
  • Function is for energy storage
37
Q

what are structural polysaccharides?

A
  • (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
Q

Polysaccharides can combine with other classes of

macromolecules to form complex polysaccharides. What are they? (2)

A

Glycoproteins - polysaccharides + proteins

Glycolipids - polysaccharides + lipids

39
Q

what is the cellular function of glycoproteins?

A

Glycoprotiens include eukaryotic cell-surface receptor molecules; typically reside on external surfaces of the membrane

40
Q

what is the cellular function of glycolipids?

A

Glycolipids important in cell walls of gram-negative bacteria

41
Q

what are triglycerides composed of?
what is its function?
what type of bonds link everything together?

A
  • 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
Q

Fatty acids consist of _________ and __________

A

carboxyl group and hydrocarbon chain

43
Q

what are saturated fatty acids?

A

no double bonds between Cs; straight, linear molecule

44
Q

what are unsaturated fatty acids?

A

one or more double bonds between the carbons; bent or kinked molecule

45
Q

what are complex lipids?

A

simple lipids that contain additional elements such as phosphorus, nitrogen, sulfur, or small hydrophilic organic compounds (e.g., sugars)

46
Q

what are phospholipids?

A

complex lipids containing 2 fatty acids, glycerol, a phosphate group and something attached to phosphate (i,.e., ethanolamine)

47
Q

why are phospholipids important?

A

play a major structural role in cytoplasmic membranes; amphipathic
*slide 45 for picture

48
Q

what is DNA? (3)

A
  • polymer of deoxribonucleotides; genetic material in all cells and some viruses
  • Double-stranded in cells, complementary strands
  • Strands held together by hydrogen bonds
49
Q

what is RNA? (3)

A
  • 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
Q

nucleotides are composed of… (3)

A

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
Q

why are nucleotides important? (4)

A
  • 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
Q

Nitrogen bases of nucleic acids belong to two chemical classes. What are they and what do they consist of?

A
  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
Q

slides 51-55

A

:)

**MAKE SURE to read slide 53; did not make into card

54
Q

what are for 4 classes RNA?

A

mRNAs, tRNAs, rRNAs, and small RNAs

55
Q

what are enzymes?

A

catalytic proteins; catalysts for chemical reactions

56
Q

what are structural proteins?

A

Integral parts of cellular structures (such as eukaryotic chromosomes)

57
Q

most amino acids consist of _____________________ 2 of 22 contain _____, 1 contains _______

A

-carbon, hydrogen, oxygen, and nitrogen; sulfur;selenium

58
Q

amino acids contain 2 important functional groups. what are they?

A

Carboxylic acid group (-COOH)
Amino group (-NH2)
*slide 59

59
Q

Adjacent amino acid monomers held together by covalent bonds called _______

A

peptide bond

60
Q

slides 60-64

A

:)

61
Q

what are isomers?

A

related, but nonidentical molecules

62
Q

what are optical isomers?

A

enantiomers (sterioisomers or mirror image isomer); have same chemical properties but often have different physical properties
*slide 66-68

63
Q

what are racemasses?

A

enzymes capable of interconverting specific enantiomers

64
Q

what is a polypeptide?

A

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
Q

Each polypeptide has an ______ end and a _____ end

A

amino; carboxyl

66
Q

what is a protein?

A

a functional unit consisting of one or more polypeptides having one or more functions.

67
Q

what is primary structure in relation to proteins/polypeptide

A

linear array of amino acids in a polypeptide

68
Q

what is secondary structure in relation to proteins/polypeptide

A

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
Q

Tertiary structure of a protein?

what does it form and why is this important?

A
  • 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
Q

tertiary structure is held together by… (4)

A

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
Q

what is the Quaternary structure of a protein?

A

overall arrangement of polypeptides in a protein; only found in proteins composed of two or more polypeptides
*slide 75-77

72
Q

what is denaturation?

A

Unfolding of Polypeptide Chains

73
Q

what can cause denaturation?

A

Extremes of pH
High temperatures
Certain chemicals

74
Q

what does denaturation result in?

A

Causes loss of biological function

75
Q

is denaturation reversible?

A

Can be reversible or irreversible

MicroBiology (17 decks)

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