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BIOLOGY 130 > Unit 2 - Cellular Chemistry/Macromolecules > Flashcards

Unit 2 - Cellular Chemistry/Macromolecules Flashcards

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1
Q

Lipid Bilayer

A

-double layered sheet of lipids which is studded with proteins
lipids
-serve as permeability barrier
-carbohydrates are attached as well
-all lipids in membrane are amphipathic
-composition varies
-form spontaneously
closed, self-sealing, important feature for cell fusion
-energetically favourable state is sealed compartment

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2
Q

Lipid aggregates in water

A

-form surface film and small micelles

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3
Q

Phospholipids

A
  • major component of cell membranes
  • polar head group and 2 hydrophobic fatty acid tails
  • two -OH groups in glycerol are linked to fatty acids, while 3rd -OH group is linked to phosphate group
  • phosphate is further linked to an alcohol
  • amphipathic
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4
Q

Unsaturated Fats

A

-one or more double bonds in hydrocarbon tail
-double bond creates kink in chain, allowing for 2 transfigurations:
1. cis - same side
2. trans - opposite side
liquid at room temp.

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5
Q

Saturated Fats

A

-no double bonds in hydrocarbon tail
-linear molecule
solid at room temp.

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6
Q

Steroids

A

-common multiple ring structure

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7
Q

Fats/Oils/Triglycerides

A

-glycerol with 3 fatty acids attached to it
long hydrocarbon chain (tail) - not very reactive
-carboxyl group (head) - behaves as an acid, chemically reactive
-stored as energy reserve through ester linkage to glycerol to form triacyglycerols

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8
Q

Functions of Carbs

A
  1. structural
  2. cell-to-cell recognition
  3. energy storage (short term)
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9
Q

Glycosidic Bonds

A
  • bond formed between -OH group on one sugar and -OH group on another through a condensation reaction - water is expelled as the bond is formed
  • bond created through condensation reaction can be broken though hydrolysis in which a water molecule is consumed
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10
Q

Cellulose

A
  • polymer of beta-glucose
  • joined by b-1,4 linkages
  • hydrogen bonding between adjacent strands
  • extremely stable, most abundant organic molecule on earth
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11
Q

Glycogen

A
  • storage form of energy in plants

- consists of highly branched a-1,4 and a-1,6 bonds

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12
Q

Geometry of bond depends on… (carbs)

A
  1. whether OH group on C1 is in alpha or beta position

2. which C of the other sugar is involved in the linkage

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13
Q

Formation of Disaccharides

A
  • monomers linked when C1 of one binds to C of another (usually C4)
  • carbon of first molecule determines structure of bond
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14
Q

Anomers of Glucose

A
  • alpha-glucose = below plane of molecule

- beta-glucose = above plane of molecule

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15
Q

Structural features of sugar monomers include…

A
  1. carbonyl group
  2. lots of -OH groups
  3. monosaccharides form rings in solution
  4. isomeric forms have identical chemical groups but are arranged differently: structural isomers (bonded to different carbons) or stereoisomers (bonded in different orientation
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16
Q

Glycolipids

A

-carbohydrates attached to lipids

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17
Q

Glycoproteins

A

-carbohydrates attached to proteins through covalent bonds

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18
Q

Polysaccharides

A

very long sugar chains

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19
Q

Monosaccharides

A

simple sugars

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20
Q

Secondary Structure of RNA

A
  • hydrogen bonds form between complementary base pairs
  • final molecule is single-stranded
  • complex folds result in some RNA having catalytic activity
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21
Q

Higher Order DNA Structure

A
  • allows for short packaging and strict regulation of gene expression
  • each DNA molecule is packaged into mitotic chromosome
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22
Q

DNA Double Helix

A
  1. stabilized by hydrogen bonds & hydrophobic interactions
  2. entire molecule is water-soluble
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23
Q

Secondary Structure of DNA

A
  • two strands of DNA align anti-parallel with bases facing inwards hydrogen bonds between bases
  • A pairs with T and C pairs with G
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24
Q

Polymerization

A
  • endergonic condensation reaction
  • involves making of new phosphodiester bonds forming 2 nucleotides
  • occurs because energy level of free nucleotides is first raised by addition of two phosphate groups
  • NTP generates NMP present in monomer
25
Q

Phosphodiester Linkage

A
  • between 5’ and 3’ carbon atoms

- joins nucleotides together

26
Q

Functions of Nucleotides

A
  1. monomeric units of RNA and DNA
  2. important signal molecules within cells
  3. important agents in energy transfer reactions of metabolism
  4. act as coenzymes/cofactors
27
Q

nucleoside

A

does not have phosphate group

28
Q

nucleotide

A
  • consists of a nitrogenous base
  • a pentose sugar
  • a phosphate group (makes nucleotide negatively charged)
29
Q

To build RNA we require…

A
  1. Phosphate group
  2. ribose sugar
  3. Base (A, U, C, G)
30
Q

To build DNA we require…

A
  1. Phosphate group
  2. Deoxyribose sugar
  3. Base (A, T, C, G)
31
Q

RNA

A
  • ribonucleic acid

- directs ordering of amino acids into peptide chain

32
Q

DNA

A
  • deoxyribonucleic acid

- sequence of subunits in DNA polymer directs RNA synthesis

33
Q

Functions of proteins`

A
  1. Enzymes –> catalyzing reactions
  2. Transport
  3. Support
  4. Signalling
  5. Movement
  6. Defense
34
Q

Misfolding

A

-many human diseases caused by this
-protein can fold properly at first, but then it may unfold —under certain conditions
when the protein misfolds, it disrupts the cell’s activity, leading to its premature death

35
Q

Renaturation

A

-when a protein is able to fold back up

36
Q

Denaturation

A

-when a protein is unfolded back to its primary structure

37
Q

4th structure of proteins

A
  • when two or more polypeptides interact to form final functional protein - isn’t always occurring
  • linked by covalent or non-covalent bonds
38
Q

2nd structure of proteins

A 
-alpha helix and beta pleated sheets
beta pleated sheets 
-can be parallel or anti-parallel
-weak hydrogen bonds in backbone
-primary structure dictates whether it gets twisted in shape
39
Q

1st structure proteins

A

-linear amino acid sequence, N-terminus (+) and C-terminus (-)

40
Q

Sickle Cell Anemia

A
  • red blood cells abnormally shaped

- when sickled, cannot fit through capillaries

41
Q

Polypeptide Chain

A
  • side chains extend from peptide-bonded backbone
  • chain is flexible, backbone is directional and asymmetrical
  • starts at N-terminus
42
Q

Peptide Bonds

A
  • covalent bonds between amino acids
  • created through condensation reaction
  • joins carboxyl carbon to amino nitrogen
  • allows bond rotation and peptide flexibility
43
Q

Hydrophilic R Groups

A
  • uncharged, but partial charges can form H bonds
  • charged, groups containing acids or bases
  • highly soluble in water
44
Q

Hydrophobic R Groups

A
  • no charged or electronegative atoms to form H bonds
  • insoluble in water
  • R groups bury themselves within polypeptide to ‘hide’ from water
  • mostly C & H
  • not very reactive
45
Q

Hybrid Amino Acid

A
  • ionized form
  • increases solubility
  • facilitates interactions with other amino acids/solutes
  • increases reactivity
46
Q

Amino Acids

A
  1. small subunits of proteins
  2. carboxylic acid & amino acid & r group
  3. connected in linear polymers of specific sequences
  4. 20 genetically encoded amino acid monomers
  5. central carbon of amino acid is referred to as ‘alpha’ carbon
  6. L-amino acids & D-amino acids, only L-amino acids are found in proteins
47
Q

Hydrolysis Reaction

A
  • chemical reaction in which water is added back across the bond
  • separating larger molecule into smaller molecules
48
Q

Condensation Reaction

A

-chemical reaction in which two or mole molecules combine and form water as a byproduct

49
Q

Base

A

-substance that accepts protons resulting in a decrease of [H+]

50
Q

Acid

A

-substance that gives up/donates protons resulting in increase of [H+]

51
Q

the longer the bond…

A

the weaker the bond

52
Q

water

A
  • most abundant molecule in biological organisms
  • known as universal solvent
  • 2 types of interactions with compounds:
    1. hydrophobic = water fearing
    2. hydrophillic = water loving
53
Q

H Bonds

A
  • electrical attraction between electronegative atom and partial positive of hydrogen
  • 3rd strongest in biological systems
54
Q

Ionic Bonds

A
  • ionic bonding
  • ionization
  • second strongest in biological systems
55
Q

Covalent Bonds

A
  • strongest bonds of biological systems
  • two or more atoms share electrons…
    1. equally - non-polar covalent bond
    2. unequally - polar covalent bond, one atom has stronger pull on electrons than the other
56
Q

4 atoms matter in organisms are made of (99%)

A
  • Carbon
  • Hydrogen
  • Oxygen
  • Nitrogen
57
Q

Regulatory Molecules

A

regulation of enzyme activity allows cell to control which enzymes are active at any time depending on the needs of the cell

58
Q

3rd structure proteins

A 
-global structure (3-D)
twisted, coiled and folded into unique shapes
-ionic interactions
-hydrogen bonds
-disulphide bonds
-covalent bonds

BIOLOGY 130 (11 decks)

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