biology chapter 3

Question 0

Hydrocarbons

Answer 0

Molecules consisting only of carbon hydrogen - stores energy

Question 1

Carbon

Answer 1

Framework of biological molecules consists primarily of carbon bonded to
Carbon, O, S, N, P or H

Can form up to 4 single covalent bonds - very versatile - forms chains, branches, rings, tubes, balls, coils

Question 2

Isomers

Answer 2

Molecules with the same molecular or empirical formula

Question 3

Structural isomers

Answer 3

Structure of carbon skeleton is different

Question 4

Stereoisomers

Answer 4

Same C skeleton but differ in how groups attached

Question 5

Enatiomers

Answer 5

Type of stereoisomer

• Mirror image molecules
• chiral molecular- when C is bonded to 4 different molecular, these can rotate either to the left or to the right - D form and L form
• D sugars and L amino acids

Question 6

Macromolecules

Answer 6

Polymers- built by linking monomers

Monomers- small similar chemical subunits

Question 7

Dehydration synthesis

Answer 7

Formation of large molecules by the removal of water

Monomers are joined to form polymers

Question 8

Hydrolysis

Answer 8

Breakdown of large molecules by the addition of water

Polymers are broken to monomers

Question 9

Carbohydrates

Answer 9

Molecules with a ratio 1:2:1 of carbon, hydrogen, oxygen

Empirical formula CH2O

C-H covalent bonds much energy
- carbohydrates are good energy storage molecules
Examples: sugars starch glucose

Question 10

Monosaccharides

Answer 10

Simplest carbohydrate- 3>6 C atoms
6 carbon sugars play important roles
Fructose is a structural isomer of glucose
Galactose is a stereoisomer of glucose enzymes. That act on different sugars can distinguish structural and strereoisomers of the basic six carbon skeleton

Question 11

Disaccharide

Answer 11

2 monosaccharides linked together by dehydration synthesis
Used for sugar transport or energy storage

Enzymes for glucose don’t recognize it attached as a disaccharide

Linkage that is connected by glycosystic

Question 12

Polysaccharides

Answer 12

Long chains of monosaccharides 
-linked through dehydration synthesis
-glycosidic linkages 
Energy storage 
plant use as starch
animals use glycogen
Structural support
plants use cellulose anthropods use as chitin
Insoluble

Question 13

Nucleus acids

Answer 13

Information molecules
Polymers- nucleus acid
Monomers- nucleotides
-sugar+ phosphate group+ nitrogenous base
-sugar is deoxyribose in DNA or ribose in RNA
Nitrogenous bases include
Purines: adenine and guanine
Pyrimidines: thymine, cytosine, uracil
Nucleotides connected by phosphodiester bonds- bonded by phosphate groups
DNA- 1 fewer oxygen
RNA-1 more oxygen

Question 14

DNA

Answer 14

Encodes information for amino acid sequence of proteins
- sequences of bases
Double helix - 2 polynucleotide strands canine tend by hydrogen bonds
- base pairing rules a with t or y in RNA
C with G

Question 15

Gene

Answer 15

Section of DNA that causes certain amino acids to bond in a certain a order = polypeptide

Question 16

RNA

Answer 16

RNA similar to DNA except
-Contains ribose instead deoxyribose OH and C2
-contains uracile instead of thymine
Single polynucleotide strand, not helical
RNA I temples from DNA
RNA uses information in DNA to specify sequence of amino acids in proteins

Question 17

Proteins functions

Answer 17

1. Enzyme catalyst
2. Defense
3. transport
4. Support
5. Motion
6. Regulation
7. storage

Question 18

Proteins

Answer 18

Proteins are polymers
-composed of 1 or more long, unbranched chains of amino acids.  
-eAch chain is a polypeptide 
Amino acids are monomers
Amino acid structure 
-central carbon atom 
-amino group
- carboxyl group 
- single hydrogen 
- variable R group

Question 19

Amino acids joined by dehydration synthesis

- peptide bond

Answer 19

.

Question 20

4 levels of structure

Part one

Answer 20

The shape of a protien determines its function and the shape is determined by the amino acid sequence

1. Primary structure - sequence of amino acids chain of amino acid= polypeptide chain
2. Secondary structure- interaction of peptide R groups and the H in peptide backbone

Question 21

4 levels of structure part 2

Answer 21

3. Tertiary structure- final fold shape of a globular protein- hydrophobic exclusion - internal amino acids are non polar( hydrophobic) and are are driven into interior of the protein and the more polar and charged are on the surface of the folded polypeptide chain
   - stabilized by a number of forces- ionic bonds, van. Der Walls forces, disulfide bridges , H bonds
   - final level of structure for proteins consisting of only a single polypeptide chain
   - quarterly structure- arrangement of individual chains (sub units) in a protein with 2 or more polypeptide chains

Question 22

Lipids

Answer 22

Loosely defined group of molecules with one main chemical characteristic

High proportion of nonpolar C-H bonds causes the molecule to be hydrophobic
Ex- fats, oils ,waxes, and even some vitamins
High energy molecules

Question 23

Fats

Answer 23

Triglycerides( triacylglycerol)
- composed of 1 glycerol and 3 fatty acids
-need not to be identical
-chain length varies
Saturated- no double bonds between carbon atoms
•higher melting point, animal origin
Unsaturated -1 or more double bond
-low melting point, plant origin
Trans fat- are artificially made with hydrogens

Question 24

Other fats

Answer 24

Terpenes- components of pigment -chlorophyll and retinal, rubber

Steroids- 4 carbon rings - cholesterol (in animals cell. Membranes ) testosterone , estrogen , prostaglandins

Question 25

Antihero sclerosis

Answer 25

Plaque adheres go the lining of blood vessels> increasing blood pressure and increase risk of stroke

Question 26

Phospholipids

Answer 26

Composed of 
- glycerol
-2 fatty acids- nonpolar " tails"
- a phosphate groups- polar" head"
Form all biological membranes

Question 27

Micelles

Answer 27

Lipids molecules orient with plar ( hydrophilic ) head toward water and nonpolar ( hydrophobic ) tails away from water