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quiz #2 Flashcards

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
CARBOHYDRATES
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
Monosaccharides
* 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
Disaccharides
* Two monosaccharides joined by a dehydration reaction * The covalent bond that results is a glycosidic linkage Different monosaccharide pairs will form different disaccharides:
25
Glucose + Fructose= sucrose
* Produced by plants * Used to move glucose to non-photosynthetic organs
26
Glucose + Galactose=lactose
* Produced by mammals as milk sugar
27
Glucose + Glucose=maltose
A product of the breakdown (hydrolysis) of starch * Used in the brewing of beer
28
Polysaccharides
* Polymers of monosaccharides, joined by glycosidic linkages * Used for glucose storage and cellular and organismal structures
29
polysacherides storage
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
polysaccharides structures
* 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
Lipids
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
Triglycerides (Fats)
* 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
“SATURATED” FAT:
* 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
unsaturated fats
* 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
multiple kinks=POLYUNSATURATED FAT
“kinks” keep molecules from packing tightly - stays thinner, fluid at room temperatures - most plant-based fats are unsaturated
36
The Phospholipid
* 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
Steroids
* 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
ANABOLIC STEROIDS:
synthetic variants of testosterone
39
protiens
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
PROTEINS: The Generic Amino Acid Monomer
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
Peptide Bond:
The covalent bond that links two amino acids
42
Polypeptide
- a linear strand of many amino acids
43
PROTEINS: Amino Acid “R”-Group Properties
* Some “R”- Groups are nonpolar, hydrophobic * Some “R”- Groups are polar or charged (hydrophilic)
44
PROTEINS: Building the Polypeptide
* 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
Protein structure -Primary (1°)
The specific sequence of amino acids in the polypeptide chain * This sequence is determined by genetic information in the DNA of chromosomes
46
prtoien structure - Secondary (2°)
* 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
protien sturcute -Tertiary (3°)
* 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
protein structure - Quaternary (4°)
* Only in some proteins * Two or more polypeptides in aggregation
49
PROTEINS: The Importance of Shape
* 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
PROTEINS: The Importance of Shape DENATURING:
* 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
Nucleic acids
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
NUCLEIC ACIDS: The Nitrogenous Bases
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
nUCLEIC ACIDS: Building the Polymer
* 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
NUCLEIC ACIDS: RNAs may exhibit base-pairing
* 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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