Chapter 2 Flashcards

(38 cards)

0
Q

Electronegative

A

Measure of the tendency of an atom to attract an electron.

Ex. F+K –> F steals e- from K
F+F –> share electrons

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1
Q

Electropositive

A

Measure of an elements ability to donate/lose an electron.

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2
Q

Ionic Bond

A
  • gain or loss of electrons
  • attraction between neg & pos e-
  • dissociate in water
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3
Q

Covalent Bond

What is needed to break them apart??

A
  • Sharing of electrons
  • strong bonds
  • require enzymes to break
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4
Q

Polar Covalent

A

-unequal sharing of electrons

Ex. Between the O & H in water molecules because the O is slightly neg & H is slightly positive.

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5
Q

Non-Polar Covalent

A

Equal sharing of electron

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6
Q

Hydrogen Bond

A
  • hydrogen atom in a polar molecule is attracted to electronegative atom in same molecule or another polar molecule
  • weakest bond

Ex. Between the O & H of separate water molecules

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7
Q

Water

A
  • polar molecule
  • excellent solvent

H2O–> OH + H+

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8
Q

Hydrophilic

A

Water loving

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9
Q

Hydrophobic

A

Water hating

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10
Q

pH

A
  • based on concentration of hydrogen

- less hydrogen —> more acidic

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11
Q

Functional Groups

A
  • determine the characteristics for a chemical reaction

- highly electronegative

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12
Q

Adenosine Triphosphate (ATP)

A
  • energy currency of a cell

- negatively charged phosphate groups repel each other and weak bonds are broken to release energy

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13
Q

Macromolecules

A

Large molecules

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14
Q

4 major classes of macromolecules

A
  • Proteins
  • Carbohydrates
  • Nucleic Acids
  • Lipids
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15
Q

Monomer examples:

A

Protiens, carbohydrates, nucleic acid, or lipids.

16
Q

Polymer

A

Monomers combined through dehydration synthesis

17
Q

Dehydration synthesis

A

Process that makes complex molecules out of simple molecules by removal of water to create bonds.

18
Q

Hydrolysis

A

Addition of water to break bonds

19
Q

Functions of Protiens

A
  • enzymes (catalyze reactions)
  • transport molecules
  • move cells
  • provide cellular framework
  • sense & respond to conditions outside cell
  • regulate gene expression
20
Q

Properties of Protiens

A
  • made up of Amino Acids
  • infinite combinations of 20 amino acid
  • protein shape determined by amino acid sequence
21
Q

What makes up a protein?

A
  • amino acid group
  • carboxyl group
  • carbon
  • unique side chain
22
Q

Peptide Bonds

A

-hold amino acids together through dehydration synthesis

23
Q

4 Protein Structures:

A
  • primary
  • secondary
  • tertiary
  • quaternary
24
Temperature's affect on protein:
Higher temp causes proteins to lose their shape because it breaks apart hydrogen bonds
25
Carbohydrates are made up of?
Polymers: - glucose - starch - cellulose DNA & RNA
26
Monosaccharides are...
Made up of chains of polysaccharides
27
Disaccharides are
Made up of two monosaccharides joined by covalent bond Ex. Sucrose (glucose+fructose) Maltose (glucose+glucose)
28
Nucleic Acids
- made up of single unite nucleotides - ribose: adenine, guanine, cytosine, & uracil - deoxyribose: adenine, guanine, cytosine, thymine
29
Nucleotides are held together by
Covalent bonds between one nucleotide's phosphate group & the sugar of the next
30
Lipids
- non polar - hydrophobic - do not dissolve in water
31
Glycerol + 3 fatty acids are combined through dehydration synthesis to create
Triglycerides
32
Glycerol + 2 fatty acids + phosphate group =
Phospholipid | Makes up cell membrane
33
Saturated fats
No double bonds
34
Unsaturated
Double bonds
35
Phospholipids contain
Hydrophilic head & hydrophobic tail
36
Lipids include...
- phospholipids - steroids - mycolic acid - triglycerides - waxes - cholesterol
37
Characteristics of Steroids? Give an example of a steroid and its function:
- hydrophobic - simple lipids - four ring structure Ex. Sterol (adds me brain stability)