Ch. 3 Molecules of Life Flashcards

1
Q

organic

A

compounds that mainly consist of carbon and hydrogen

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2
Q

non-organic

A

molecules that have no carbon atoms

ex. water

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3
Q

Why study carbon?

A

Carbon’s outer shell has only 4 electrons which allows carbon to make pretty stable covalent bonds with other elements

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4
Q

How do carbon atoms bond?

A

3-dimensionally

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5
Q

hydrocarbon

A

carbon chain with only hydrogen attached, completely non-polar

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6
Q

carbon bonds

A
  • single
  • double
  • triple
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7
Q

Single carbon bonds

A
rotates easily 
ex. single bonded straight carbon chain:
    H H H H
H-C-C-C-C-H
    H H H H
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8
Q

double carbon bonds

A
moderate movement
ex. double bonded carbon chain:
H         H
    C=C
H         H
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9
Q

triple carbon bonds

A

restricted movement
ex. triple bond
H- C≡C-H

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10
Q

branched carbon chain

A

H H H H
H-C-C-C-C-H
H H | H
H -C -H

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11
Q

ringed carbon chain

A

example:

            H
H         C        H
     C           C
     C           C
H         C         H
            H
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12
Q

functional groups

A
an atom (other than hydrogen) or small molecular group that covalently bonds to the carbon backbone of an organic compound
ex. carboxyl group
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13
Q

What do functional groups do?

A

functional groups give organisms it its different structure and function
ex. estrogen and testostorone

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14
Q

Types of metabolic reactions (that we’ll study most)

A
  • condensation

- hydrolysis (cleavage)

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15
Q

condensation reaction

A

2 molecules covalently combine to form a larger molecule by addition of heat and release of water
subunits=polymer
A+B=AB

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16
Q

hydrolysis (cleavage) reaction

A

a large molecule splits into two smaller molecules by addition of water
polymer=-subunits
AB=A+B

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17
Q

Macromolecules

A
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids
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18
Q

What are carbohydrates?

A

most abundant of all biological molecules

  • structure: C,H,O in a 1:2:1 ratio
    uses: structural material, stored energy, transportable energy
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19
Q

Types of carbohydrates

A
  • monosaccharides
  • disaccharides
  • polysaccharides
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20
Q

Monosaccharides

A
(simple sugars)
simplest carbohydrates
- are the main energy source for most organisms
-sweet tasting, water soluble
-most have 5- or 6- carbon backbone
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21
Q

examples of monosaccharides

A

glucose (6C)
fructose (5C)
ribose (5C)
deoxyribose (5C)

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22
Q

Disaccharides

A

(double sugar)

  • *short chain carbohydrates**
  • formed by condensation reaction
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23
Q

examples of disaccharides

A

lactose, maltose, and (sucrose- most plentiful in nature)

*glucose+fructose=sucrose**

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24
Q

Polysaccharides

A

(complex sugars)

  • straight/ branched chains of many sugar monomers (3+)
  • -composed entirely of glucose
25
examples of polysaccharides
cellulose (tough, indigestible plant fibers: celery) starch (amylose in grains, potato and pasta) ***takes longer to digest** chitin: forms external skeleton/ hard body parts in many animals (ex. crabs, earthworms, insects, ticks) **also found in fungi
26
glycogen
sugar storage polysaccharide molecule in muscles and liver of animals * **only sugar storing molecules in animals*** * can be broken into glucose when blood sugar drops*
27
Lipids
(fats) structure: a glycerol with 1,2, or 3 fatty acid tails - doesn't dissolve easily in water; also hydrophobic and non-polar uses: cell membrane structure, energy storage, signal molecules, water proofing covering
28
examples of lipids
- saturated fats - monounsaturated - polyunsaturated - triglycerides - waxes - sterols
29
lipids and fatty acid types
-with fatty acid tail: fats/triglycerides, phospholipid, waxes, saturated, monounsaturated, polyunsaturated -no fatty acid tail: sterols
30
Saturated fats
(single bonded only) - solid at room temperature - don't break down easily; fully saturated with hydrogen ex. beef fat, pork fat, lard, butter
31
Monounsaturated fats
(carbon chain has 1 or more double bonds) - liquid at room temperature - breaks down easier; not fully saturated with hydrogens ex. olive oil, cheese, nuts, eggs
32
Polyunsaturated fats
(carbon chain with at least 3 double bonds) - best for your health: easier to digest ex. seeds, soybeans, avocado
33
Triglycerides
consists of a glycerol and 3 fatty acid tails - neutral fat -most abundant lipid in human body - richest energy source (9cal/gm) uses: insulation, fat storage, protection of bones and internal organs
34
Phospolipids
consists of a glycerol with a phosphate head and 2 fatty acid tails -creates the phospholipid bilayer in the cell - maintains homeostasis in the cell: regulates what enters/exists the cell
35
Waxes
- firm consistency: repel water - waterproofing in plants/animals ex. cuticles on fruit, veggies, leaves; beeswax, earwax, skin, hair, feathers
36
dessication
action of drying, removal of moisture
37
Sterols
(lipids with no fatty acid tail) - four carbon ring with functional groups - regulates hormone and vitamin production ex. cholesterol, hormones, steroids, bile salts, vitaminD
38
cholesterol
most common sterol in animals (made by liver) and obtained through diet -too much can lead to atherosclerosis
39
**atherosclerosis** | not that important to know completely
**deposits of plaque (fatty material) on the walls of blood vessel that constricts the flow of blood through the veins and arteries-- can lead to heart disease**
40
sterols and hormones
give rise to secondary sexual characteristics and gamete formation ex. estrogen and testosterone
41
Proteins (pt1)
chain of amino acids held by/linked together by peptide bonds (called a polypeptide) * proteins determine the structure and functions of organisms * *20 different kinds of amino acids make up 100 million particles
42
Proteins (pt2)
structure dictations function: - 3 dimensional shape of protein determines its biological function - primary structure - secondary structure - tertiary structure - quaternary structure
43
primary structure
linear chain of amino acids (polypeptide)*type of protein | -[]-[]-[]-[]-[]-[]-[]
44
secondary structure
polypeptide folds in helices/folded sheets /\/\/\/\/\/\/\/\/\/\/\ /\/\/\/\/\/\/\/\/\/\/\
45
tertiary structure
further folding of helices or sheet into loop | -these sheets make a protein a "working molecule"
46
quaternary structure
two or more polypeptide held into a globule for a particular shapes for a specific function
47
fibrous protein
chains arranged as strands or sheets | ex. keratin, collagen
48
major types of proteins
- structural - regulatory - hormones - transport - antigens - enzymes
49
structural proteins
make up cell parts, keratin in skin and hair, feathers, webs, bones and cartilage
50
regulatory proteins
controls the individual parts of cell (organelles)
51
hormone proteins
"molecular messages" that control growth and developement
52
transport proteins
carry substances throughout body | ex. hemoglobin
53
antigen proteins
cause formation of antibodies which provide protection from disease *specific to their antigen
54
enzyme protein
special proteins that act as a catalyst to speed up reactions
55
polypeptides may have organic compounds attached like:
- lipoproteins: proteins combined with lipids/fats | - glycoproteins: proteins combined with sugars
56
denaturation
disruption of 3 dimensional shape of a protein - will cause a protein to no longer function properly * causes of denaturation: pH, temperature
57
Nucleic acids
``` (DNA or RNA) rna- single coil (ribose sugar) dna- double coil (deoxyribose sugar) -both consist of nucleotides (sugar, phosphate, and nitrogen base ```
58
nitrogen bases
purines: adenine or guanine *double unit pyrimidines: thymine or cytosine *single unit (thymine is replaced by purine: uracil in RNA)
59
purine and pyrimidines
purines join with pyrimidines to joint the two sides of DNA molecules in the following order ONLY: A-T G-C