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quiz #2 Flashcards

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1
Q

How many covalent bonds can form with carbon

A

up to 4 other atoms

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2
Q

In organic chemistry, carbon forms the basis for
molecular structure, what is the name it is given

A

carbon skeleton

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3
Q

Hydrocarbons

A

-Organic molecules consisting only of hydrogen and carbon
- Dominated by nonpolar covalent bonds (hydrophobic)
- Some biological molecules have major hydrocarbon regions

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4
Q

Isomers

A

organic molecules with the same molecular formula but
different structural arrangements
- different structures can result in different properties
- seemingly minor differences can have profound biological effects

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5
Q

structural isomers

A

differ in the covalent arrangement of the atoms

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6
Q

cis-trans isomers

A

differ in the arrangement around carbon to carbon double bond
cis-the two X’s are on the same side
trans- the two X’s are on opposite sides

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7
Q

enantiomers

A

mirror images- due to one carbon being asymmetric it is attached to 4 diff atoms or groups
-important in detecting different scents

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8
Q

fill in the blanks
- carbon forms the basis for molecular

A
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8
Q

fill in the blanks
- carbon forms the basis for molecular

A
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8
Q

fill in the blanks
- carbon forms the basis for molecular

A
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8
Q

fill in the blanks
- carbon forms the basis for molecular_____

A

structure

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9
Q

fill in the blank
Isomeric arrangements can influence______

A

function

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10
Q

functional groups

A

small chemical groups
attached to the carbon skeleton – are the key to
both function and chemical interactions

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11
Q

Hydroxyl group (—-OH)

A

STRUCTURE:
* Oxygen and one hydrogen
FUNCTIONAL PROPERTIES:
* Polar – electronegative oxygen creates
partial charges (δ– and δ+)
NAME OF GROUPS/COMPOUNDS:
* Alcohols have one –OH group

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12
Q

carbonyl group (>C=O)

A

STRUCTURE:
* One carbon of the “carbon skeleton” double-bonded to an oxygen
FUNCTIONAL PROPERTIES:
* Weakly polar due to electronegative oxygen
NAME OF GROUPS/COMPOUNDS:
* Ketones: carbonyl is within the carbon chain
* Aldehydes: occurs at the end of the chain

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13
Q

carboxyl group (—-COOH)

A

STRUCTURE:
* “Side chain” or at the end of a carbon chain
* one carbon double-bonded to one oxygen and
bonded to an OH group (also written ─COOH)
FUNCTIONAL PROPERTIES:
* Acts as an acid – donates one H+
NAME OF GROUPS/COMPOUNDS:
* Carboxylic Acids

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14
Q

amino group (—NH2)

A

STRUCTURE:
* Nitrogen and two hydrogen atoms
FUNCTIONAL PROPERTIES:
* Acts as a base – the nitrogen can bind up
one H+ proton (forms —NH3
+
)
NAME OF GROUPS/COMPOUNDS:
* Amines

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15
Q

sulfhydryl group (—SH)

A

STRUCTURE:
* Sulfur and one hydrogen
FUNCTIONAL PROPERTIES:
* Two sulfhydryl groups can create a covalent
bond in a disulfide bridge
* These stabilize some protein structures

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16
Q

methyl group (—-CH3)

A

STRUCTURE:
* “Side chain” or at the end of a carbon chain
* One carbon bonded to three hydrogens
FUNCTIONAL PROPERTIES:
* Nonpolar – due “nonpolar covalent bonds”
NAME OF GROUPS/COMPOUNDS:
* Methylated Compounds have had methyl
groups added to their normal structure

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17
Q

Phosphate group (—OPO3 2-)

A

STRUCTURE:
* Phosphorus attached to 4 oxygen atoms
(one oxygen is bonded to the carbon skeleton)
* Also written ─PO4
FUNCTIONAL PROPERTIES:
* Strong negative charges
NAME OF GROUPS/COMPOUNDS:
* Phosphates
ROLE IN CELL ENERGETICS:
Adenosine Tri-Phosphate (ATP).* ATP provides chemical
energy to run specific
reactions in the cell
* The bond to the third
phosphate represents a
significant amount of energy

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18
Q

fill in the blank
Macromolecules are first formed as _______: a long chain of
linked smaller molecules s (___)

A

polymers
monomers

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19
Q

Cells use similar chemical reactions
in the building (______) of large polymers, and for
breaking down (______) of polymers into separate monomers

A

synthesis
digestion

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20
Q

Monomers are linked together by a DEHYDRATION REACTION:

A

Occurs at one hydrogen and a
the hydroxyl group (or two hydroxyl
groups )
* A water molecule is removed as
the bond is formed

21
Q

Polymers are broken down to
release monomers by
HYDROLYSIS:

A

One water molecule is used
* The bond is broken, forming a
hydroxyl group and a hydrogen
at the break

22
Q

CARBOHYDRATES

A

Include: Sugars and polymers of sugars
* MONOSACCHARIDES (simple sugars)
– direct source of cellular energy
* DISACCHARIDES (short-chain “double” sugars)
– naturally-produced sugar compounds (in plants, milk)
* POLYSACCHARIDES (complex polymer sugars)
– a way to store simple sugars
and build cellular structures
Properties:
* Contain C, H, and O
* Most are polar due to hydroxyl groups (−OH)

23
Q

Monosaccharides

A
  • Generic Molecular Formula = CXH2XOX
  • Monosaccharides can be ketone sugars (“ketoses”) or
    aldehyde sugars (“aldoses”)
    * The hexoses (C6H12O6
    ) are important structural isomers
  • Glucose is the main sugar for cellular energy
  • Galactose, fructose are also used, but require extra chemical reactions
  • You can taste the difference between the aldoses and ketoses
  • Hexose and pentoses form rings in aqueous solutions:
  • Different isomers form different ring structures
    Fructose has a different ring structure
24
Q

Disaccharides

A
  • Two monosaccharides joined by a dehydration reaction
  • The covalent bond that results is a glycosidic linkage
    Different monosaccharide pairs will form different disaccharides:
25
Q

Glucose + Fructose= sucrose

A
  • Produced by plants
  • Used to move glucose
    to non-photosynthetic
    organs
26
Q

Glucose + Galactose=lactose

A
  • Produced by mammals
    as milk sugar
27
Q

Glucose + Glucose=maltose

A

A product of the
breakdown (hydrolysis)
of starch
* Used in the brewing of
beer

28
Q

Polysaccharides

A
  • Polymers of monosaccharides, joined by glycosidic linkages
  • Used for glucose storage and cellular and organismal structures
29
Q

polysacherides storage

A

STORAGE:
Starch
* Produced by plants
* Amylose: unbranched
polymer
* Amylopectin:
polymer chains with
some branching
Glycogen:
Produced by
animals (esp.
mammals)
* Highly branched
polymer of glucose
* Stored in liver &
muscles

30
Q

polysaccharides structures

A
  • Plants create a complex polysaccharides called cellulose
  • Cellulose uses a slightly different isomer called β- (Beta-) Glucose
  • β-Glucose permits “cross-links” between strands
  • (Starch & glycogen form linkages with α- (alpha-) glucose; no crosslinks)
31
Q

Lipids

A

Include: Fats and other hydrophobic organic compounds
* TRIGLYCERIDES (Fats)
– stored energy; insulation, cushioning
* PHOSPHOLIPIDS
– basis for all cell membranes
* STEROIDS
– four-ring carbon skeleton
– precursor for hormones and vitamins
Properties:
* Mostly C and H, with very little O
* Dominated by nonpolar covalent bonds

32
Q

Triglycerides (Fats)

A
  • Carbon double-bonds change the physical structure of fatty acid chains:
  • For this fat, there is one
    covalent bond between all of
    the carbons
  • Each carbon in the chain is
    bonded to two hydrogens
33
Q

“SATURATED” FAT:

A
  • No double-bonds
  • It is “saturated” with hydrogen
  • Carbon chain is straight
    -“packs” together
  • stays thicker, solid
    at room temperature
  • most animal fats
    are saturated fats
34
Q

unsaturated fats

A
  • For this fat, note the double
    covalent bond between one
    carbon pair
  • These two carbons only bond
    to one hydrogen each
    At least one cis double-bond
  • Fewer hydrogens: “unsaturated”
  • Carbon chain has a “kink” at
    the double bond
35
Q

multiple kinks=POLYUNSATURATED FAT

A

“kinks” keep
molecules from
packing tightly
- stays thinner, fluid at
room temperatures
- most plant-based
fats are unsaturated

36
Q

The Phospholipid

A
  • A molecule with ‘hybrid’ properties:
  • A triglyceride with one fatty acid removed
  • It is replaced by a phosphate group (negative charge) attached to a
    positive-charged side group
  • Phospholipids spontaneously form a bilayer in water
  • The hydrophilic heads are attracted to water
  • The hydrophobic tails are repelled by water
37
Q

Steroids

A
  • Four, flat, interconnected rings of carbon form the “skeleton”
  • Cholesterol: the most important of the steroids:
  • Helps to form Vitamin D, steroid hormones, bile
38
Q

ANABOLIC STEROIDS:

A

synthetic
variants of testosterone

39
Q

protiens

A

Properties:
* Each protein is a polymer of
monomer subunits called Amino Acids
* Many amino acids are joined in a
chain called a polypeptide
* There are 20 different amino acids
that can be used to make a polypeptide
* Each polypeptide must be coiled,
folded and shaped to achieve a final
functional shape…
PROTEIN SHAPE DETERMINES
PROTEIN FUNCTION

40
Q

PROTEINS: The Generic Amino Acid Monomer

A

The “R”-group:
* “R” is a symbolic placeholder
* It is a variable side-chain that differs among
the 20 amino acids amino acids
* The “R”-group gives each of the
20 amino acids its own structure
and properties
* The amino and carboxyl groups
are where amino acid monomers
are linked together

41
Q

Peptide Bond:

A

The covalent bond that links
two amino acids

42
Q

Polypeptide

A
  • a linear strand of many amino acids
43
Q

PROTEINS: Amino Acid “R”-Group Properties

A
  • Some “R”- Groups are nonpolar, hydrophobic
  • Some “R”- Groups are polar or charged (hydrophilic)
44
Q

PROTEINS: Building the Polypeptide

A
  • The 20 amino acids can be “strung together” in many different ways
  • Each protein can have 100s or 1000s of amino acids
  • RESULT: an organism can make thousands of different proteins
    using just twenty monomers
  • The sequence of amino acids makes each protein unique
  • This sequence determines how it coils and folds into a final shape
45
Q

Protein structure -Primary (1°)

A

The specific sequence of amino
acids in the polypeptide chain
* This sequence is determined by
genetic information in the DNA of
chromosomes

46
Q

prtoien structure - Secondary (2°)

A
  • Different sections
    (“domains”) of the polypetide
    are coiled into an α-(alpha-)
    helix, or folded into a β-(beta-)
    pleated sheet
  • These ‘generic’ structures
    are due to hydrogen bonding
    between parts of the
    polypeptide ‘backbone’
47
Q

protien sturcute -Tertiary (3°)

A
  • The folding and bending of the
    protein to arrange domains into a
    stable, specific final shape
  • Due to attractions among “R”-
    group side chains, including:
  • Hydrogen bonding
  • Hydrophobic interactions
  • Ionic bonds
  • Covalent bonds (disulfide
    bridges)
48
Q

protein structure - Quaternary (4°)

A
  • Only in some proteins
  • Two or more polypeptides in
    aggregation
49
Q

PROTEINS: The Importance of Shape

A
  • This is the enzyme
    “lysozyme”
  • A special ‘groove’ that
    matches a bacterial cell
    wall molecule allows
    lysozyme to bind to and
    destroy bacteria
  • An antibody protein
    matches a foreign virus to
    enable destruction by the
    immune system
50
Q

PROTEINS: The Importance of Shape
DENATURING:

A
  • Proteins must maintain their
    specific shape to function
  • If they unravel or otherwise lose
    their higher level shapes
    (DENATURE), they cease to be
    able to function
51
Q

Nucleic acids

A

INclude=
DNA: The ‘Information’ Molecule
− The molecule of inheritance
− Carries coded information (genes) for the amino acid sequences
(1º-level structures) of all of an organism’s proteins
− Structure: Double-stranded molecule
RNA : The ‘Synthesis’ Molecule
− The molecule of protein synthesis
− RNA directs the assembly of proteins encoded in the DNA
− Structure: Single-stranded moleculeProperties:
* Strong negative charge due to phosphate groups on monomers
* The genetic code in DNA that determines primary protein structure is
essentially universal among all life forms

52
Q

NUCLEIC ACIDS: The Nitrogenous Bases

A

Each base is characterized by a chemical ring structure made up
of carbon and nitrogen.
PYRIMIDINES (1 ring):
▪ Cytosine (C)
▪ Thymine (T) – DNA only
▪ Uracil (U) – RNA only
PURINES (2 rings):
▪ Adenine (A)
▪ Guanine (G)
The ‘coded information’ is read in the sequence of bases

53
Q

nUCLEIC ACIDS: Building the Polymer

A
  • A phosphate group links the
    sugars of two nucleotides:
    The phosphate group attaches
    to the #5 carbon on one sugar,
    and the #3 carbon on the next
  • The end of a strand the ends with
    the sugar is the 3’-end
  • The end of a strand with the
    phosphate group is the 5’-end
  • This forms the sugar-phosphate
    backbone of a nucleic acid
    RNA is typically a single strand of nucleotides
  • DNA occurs as two strands in a double helix
  • Covalent bonds link
    nucleotides in the “sugarphosphate backbone”
  • In DNA, two strands twist
    around each other in a “double
    helix”
    -The strands are linked
    together by hydrogen bonds
    between complementary base
    pairs:
54
Q

NUCLEIC ACIDS: RNAs may exhibit base-pairing

A
  • Some RNA molecules may
    form complementary base
    pairing within the same
    strand
  • For RNA, complementary
    base pairs are:
    A···U
    U···A
    C···G
    G···C

Bio Quiz #2 (1 decks)

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