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A&P : Unit 1 > Chapter 2.2 : Organic Chemistry > Flashcards

Chapter 2.2 : Organic Chemistry Flashcards

1
Q

Organic Chemistry

A

Study of compounds containing carbon and hydrogen

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2
Q

What are the four categories of organic compounds?

A

– carbohydrates
– lipids
– proteins
– nucleic acids

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3
Q

Monomers

A

a small identical molecules (similar
subunits) - e.g. amino acid or glucose molecule

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4
Q

Polymers

A

molecules made of a repetitive series
of identical subunits // e.g. polypeptide

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5
Q

Macromolecules

A

– polymers which continue to
“enlarge” to form very large organic molecules //
high molecular weights /// e.g. protein

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6
Q

Organic

A

molecules with carbon and hydrogen

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7
Q

Carbon has _ valence electrons

A

4

– may bind with four other atoms
– these atoms provide carbon with four more electrons to fill its
valence shell // making carbon’s valence orbit “stable”
– forms covalent bonds with hydrogen, oxygen, nitrogen, sulfur,
and other elements

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8
Q

Carbon atoms also bind readily with

A

each other

– forms branches and ring structures /// forms a carbon chain or
carbon backbones
– able to form 3D matrix (e.g. pencils & diamonds)

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9
Q

Carbon is the _____ that carries a variety of functional groups

A

backbone

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10
Q

Functional Groups

A
  • small clusters of atoms
    attached to carbon
    backbone
  • determines many of the
    properties of organic
    molecules
  • E.g. = hydroxyl, methyl,
    carboxyl, amino, phosphate
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11
Q

Dehydration synthesis

A

Process where monomers are joined together to form a polymer

(condensation) is how living cells form
polymers

– a hydroxyl (-OH) group is removed from one monomer, and
a hydrogen (H+) from another /// producing water as a byproduct

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12
Q

Hydrolysis

A

Splitting a polymer (lysis) by the addition of a water
molecule (hydro) // a covalent bond is broken

All digestion reactions consists of hydrolysis reactions

– a water molecule ionizes into –OH and H+
– the covalent bond linking one monomer to the other is
broken
– the –OH is added to one monomer
– the H+ is added to the other

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13
Q

Carbohydrates

A

A hydrophilic organic molecule

general formula // note: 2:1 ratio for hydrogen to oxygen

names of carbohydrates often built from:
– word root ‘sacchar-’
– the suffix ’-ose’
– both mean ‘sugar’ or ‘sweet’ // monosaccharide or glucose

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14
Q

Monosaccharides

A

Simple carbohydrates = simple sugars

glucose, galactose and fructose

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15
Q

glucose

A

is blood sugar

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16
Q

Disaccharides

A

Sugar molecule composed of 2
monosaccharides

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17
Q

sucrose

A

table sugar //
glucose + fructose

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18
Q

lactose

A

sugar in milk //
glucose + galactose

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19
Q

maltose

A

grain products //
glucose + glucose

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20
Q

Polysaccharides

A

Long chains of glucose molecules

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21
Q

Three important polysaccharides

A

(glycogen – starch - cellulose)

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22
Q

Glycogen

A

energy storage polysaccharide in animals

  • made by cells of liver, muscles, brain, uterus, and vagina
  • liver produces glycogen after a meal when glucose level is
    high, then breaks it down between meals to maintain blood
    glucose levels
  • muscles store glycogen for own energy needs
  • uterus “sweats” glycogen to nourish embryo
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23
Q

Starch

A

energy storage polysaccharide in
plants /// only significant digestible
polysaccharide in the human diet

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24
Q

Cellulose

A

structural molecule of plant cell
walls /// this is the “fiber” in our diet our
digestive system lack enzymes to breakdown
this polymer passes out of our digestive system
as food residue

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25
Q

Carbohydrate Functions

A
  • Source of energy // all digested carbohydrates converted to glucose // oxidized to make ATP
  • Structural molecule when conjugated (i.e. bonded to) with lipids or proteins
    – glycolipids // e.g. component of cell membrane with lipid
    inserted into membrane and sugar projecting from surface of
    membrane
    – glycoproteins // e.g. component of cell membrane with protein
    inserted into membrane and sugar projecting from surface of
    membrane Carbohydrate Functions
    – proteoglycans (mucopolysaccharides) // forms gel between
    cells – its the “glue that binds cells and tissues together
    • forms gelatinous filler in umbilical cord and eye
    • joint lubrication
    • seen as the tough, rubbery texture of cartilage
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26
Q

Lipids

A

Hydrophobic organic molecule
– composed of carbon, hydrogen and oxygen
– with high ratio of hydrogen to oxygen

Less oxidized than carbohydrates, and therefore
has more calories/gram

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27
Q

Five primary human lipids

A

– fatty acids
– triglycerides
– phospholipids
– eicosanoids
– steroids

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28
Q

Fatty Acids

A
  • Chains of 4 to 24 carbon atoms // carboxyl (acid) group on one end,
    methyl group on the other and hydrogen bonded along the sides
  • Classified as:
    – saturated – all carbon atoms saturated with hydrogen
    – unsaturated - contains C=C bonds without hydrogen
    – polyunsaturated – contains many C=C bonds
    – essential fatty acids – obtained from diet, body can not
    synthesize
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29
Q

Triglycerides (Neutral Fats)

A
  • Three fatty acids covalently bonded to a three carbon alcohol (a glycerol molecule)
    – each bond formed by dehydration synthesis
    – once joined to glycerol /// fatty acids can no longer donate protons – it is a neutral fats
    – maybe broken down by hydrolysis
  • Triglycerides when at room temperature
    – If liquid its called an oils // often polyunsaturated fats from
    plants
    – If solid its called a fat // saturated fats from animals
  • Primary Function - energy storage, insulation and shock
    absorption (adipose tissue)
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30
Q

Phospholipids

A

similar to neutral fat except
that one fatty acid replaced
by a phosphate group
* structural foundation
of cell membrane

Amphilphillic

– fatty acid “tails” are
hydrophobic // water
fear
– phosphate “head” is
hydrophilic // water
seaking

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31
Q

Amphiphilic

A

single molecule containing both a neutral and charged region

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32
Q

Width of a Plasma Membrane

A

5.5 to 7.5 nm Thick

Approximately 25 water
molecules are needed
to span the width of a
plasma membrane!

33
Q

Diameter of
water molecule =

A

0.29 nm

34
Q

Eicosanoids

A
  • 20 carbon compounds derived from a fatty acid called
    arachidonic acid
  • hormone-like chemical signals between cells
  • includes prostaglandins – produced in all tissues
    – role in inflammation, blood clotting, hormone action,
    labor contractions, blood vessel diameter
35
Q

Steroid

A

a lipid with 17 of its carbon atoms in four rings

36
Q

Cholesterol

A

the ‘parent’ steroid from which the other steroids
are synthesized

– E.g. cortisol, progesterone, estrogens, testosterone and bile
acids

– synthesized only by animals // especially liver cells // 15%
from diet, 85% internally synthesized
– important component of cell membranes
– required for proper nervous system function
– never metabolized for energy!

37
Q

“Good” and “Bad” Cholesterol

A

‘Good’ and ‘bad’ cholesterol refers to two different
transporter “types” associated with the blood

38
Q

“good” cholesterol”

A

HDL – high-density lipoprotein
– lower ratio of lipid to protein in its shell
– may help to prevent cardiovascular disease

39
Q

“bad” cholesterol”

A

LDL – low-density lipoprotein
– high ratio of lipid to protein in its shell
– contributes to cardiovascular disease

40
Q

Proteins

A

a polymer of amino acids

Greek word meaning “of first importance” // most versatile
molecules in the body /// organic molecule

41
Q

Amino acid

A

central carbon with 3 attachments // amino group
(NH2), carboxyl group (COOH) and radical group (R group)

20 amino acids used similar “backbone” to make the proteins but unique radical (R) group
– properties of amino acid determined by -R group
– amino acids are defined as either essential or non-essential

42
Q

Peptide

A

any molecule composed of two or more
amino acids joined by peptide bonds

43
Q

Peptide bond

A

joins the amino group of one amino
acid to the carboxyl group of the next
– formed by dehydration synthesis

44
Q

Peptides named for the number of amino acids

A

– dipeptides have 2
– tripeptides have 3
– oligopeptides have fewer than 10 to 15
– polypeptides have more than 15
– proteins have more than 50

45
Q

Dipeptide Synthesis

A

Dehydration synthesis creates a peptide bond that joins amino acids // covalent
bond between carbon and nitrogen = peptide bond

46
Q

Primary protein structure

A

protein’s sequence amino acid which is encoded in the
genes

47
Q

Secondary protein structure

A

coiled or folded shape held together by hydrogen
bonds
– hydrogen bonds between slightly negative C=O and
slightly positive N-H groups
– most common secondary structure are:
* alpha helix – springlike shape
* beta helix – pleated, ribbonlike shape

48
Q

Tertiary structure

A

further bending and folding of proteins into globular and
fibrous shapes

49
Q

globular proteins

A

compact tertiary structure well
suited for proteins embedded in cell membrane and
proteins that must move about freely in body fluid

50
Q

fibrous proteins

A

slender filaments better suited for
roles as in muscle contraction and strengthening the
skin

51
Q

Quaternary structure

A

– associations of two or more separate polypeptide chains
– functional conformation – three dimensional shape

52
Q

prosthetic group

A

Proteins that contain a non-amino acid moiety are called a

53
Q

Hemoglobin contains four complex iron containing rings called

A

heme moieties

54
Q

Conformation

A

unique three dimensional shape of
protein crucial to function

– Some proteins have ability to reversibly change their
conformation – important in:
* enzyme function
* muscle contraction
* opening and closing of cell membrane pores

55
Q

Denaturation

A

extreme conformational change that
destroys function and protein can not revert back to its
original shape // caused by extreme heat, pH or agitation

56
Q

Proteins Have Many Functions

A
  • Structure
    – keratin – tough structural protein
    • gives strength to hair, nails, and skin surface
      – collagen – durable protein contained in deeper layers of skin,
      bones, cartilage, and teeth
  • Communication
    – some hormones and other cell-to-cell signals
    – receptors to which signal molecules bind
    * ligand – any hormone or molecule that reversibly binds to
    a protein
  • Membrane Transport
    – channels in cell membranes that governs what passes through
    – carrier proteins – transports solute particles to other side of
    membrane
    – turn nerve and muscle activity on and off
  • Catalysis
    – enzymes
  • Recognition and Protection
    – immune recognition
    – antibodies
    – clotting proteins
  • Movement
    – motor proteins - molecules with the ability to change shape repeatedly
  • Cell adhesion
    – proteins bind cells together
    – immune cells to bind to cancer cells
    – keeps tissues from falling apart
57
Q

Enzymes

A

proteins that function as biological catalysts

– permit reactions to occur rapidly at normal body temperature

58
Q

Substrate

A

substance that the enzyme acts upon

59
Q

Naming Conventions

A

– named for substrate with -ase as the suffix (e.g. amylase =
enzyme that digests starch (note difference for amylose ///
“ose” indicates sacharide – amylose polymer of glucose)

60
Q

Enzymes lower activation energy

A
  • energy needed to get
    reaction started /// enzymes facilitate molecular interaction
61
Q

Enzymes are reusable

A

enzymes are not consumed by the
reactions

62
Q

one enzyme molecule may consume

A

millions of substrate molecules per minute

Astonishing speed

63
Q

Factors that change enzyme shape

A

– pH, temperature, agitation
– alters or destroys the ability of the enzyme to bind to substrate
– enzymes action have optimum pH /// salivary amylase works
best at pH 7.0 /// pepsin works best at pH 2.0
– temperature optimum for human enzymes – body temperature
(37 degrees C

64
Q

Enzymes Control Metabolic Pathways

A

Chain of reactions // each step catalyzed by a different enzyme

65
Q

Nucleotides

A

Organic Molecules

66
Q

Three components of a nucleotide

A

– nitrogenous base (single or
double carbon-nitrogen ring)
– sugar (monosaccharide)
– one or more phosphate groups

67
Q

ATP is the best know

A

nucleotide

68
Q

DNA

A
  • 100 million to 1 billion nucleotides long
  • Our genes are constructed from DNA
    – instructions for synthesizing all of the body’s
    proteins
    – transfers hereditary information from cell to
    cell and generation to generation
    – DNA codes for protein // either a structural
    molecule or an enzyme (enzymes can make
    other organic molecules)
69
Q

RNA

A
  • messenger RNA, ribosomal RNA, transfer RNA
  • 70 to 10,000 nucleotides long
  • carries out genetic instruction for synthesizing proteins
  • assembles amino acids in the right order to produce
    proteins
  • single strand // not double stranded like DNA
  • Micro-RNA // functions as a biocatalyst
70
Q

Adenosine Triphosphate (ATP)

A
  • body’s most important energy-transfer molecule // the molecule
    which provides energy for all cellular work // “molecular money”
  • briefly stores energy gained from exergonic reactions
  • releases it within seconds for physiological work // ATP not used
    to store energy
  • holds energy in covalent bonds
    – 2nd and 3rd phosphate groups have high energy bonds //
    denoted by this symbol “ ~ “
    – most energy transfers to and from ATP involve adding or
    removing the 3rd phosphate
71
Q

Adenosine triphosphatases (ATPases)

A

hydrolyze the 3rd high energy phosphate bond
– separates into ADP + Pi + energy

72
Q

Phosphorylation

A

– addition of free phosphate group to ADP molecule
– carried out by enzymes called kinases (phosphokinases)
– ATP can be formed by directly phosphorylation of ADP (substrate level phosphorylation) or by a mechanism within mitochondria called oxidation-phosphorylation which requires using an electron chain and ATP-synthetase

73
Q

ATP contains

A

adenine, ribose and 3 phosphate groups

74
Q

Overview of ATP Production

A

ATP consumed within 60
seconds of formation
* entire amount of ATP in
the body would support
life for less than 1 minute
if it were not continually
replenished
* cyanide halts ATP
synthesis // stops
electrons from moving
down electron transport
chain which is inside the
mitochondria

75
Q

Guanosine triphosphate (GTP)

A

– another nucleotide involved in energy transfer
– donates phosphate group to other molecules

76
Q

Cyclic adenosine monophosphate (cAMP)

A

– nucleotide formed by removal of both second and
third phosphate groups from ATP
– formation triggered by hormone binding to cell
surface
– cAMP becomes “second messenger” within cell
– activates metabolic effects inside cell

77
Q

Cofactors

A

– about 2/3rds of human enzymes require a non-protein
cofactor
– inorganic partners (iron, copper, zinc, magnesium and
calcium ions)
– some bind to enzyme and induces a change in its
shape, which activates the active site
– essential to function

78
Q

Coenzymes

A

organic cofactors derived from water-soluble vitamins
(niacin, riboflavin)

– they accept electrons from an enzyme in one metabolic
pathway and transfer them to an enzyme in another metabolic
pathway /// This is an Oxidation-Reduction Reaction
– the molecule losing the electron is “oxidized” and the molecule
gaining the electron is “reduced” (i.e. redox reaction)
– The electron carrier is reqired by the enzyme to catalyze the
reaction reaction (e.g AB —–> A + B)
– NAD to NADH or FAD to FADH are examples of electron
carriers

A&P : Unit 1 (11 decks)

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