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Cliffs AP Bio > Chapter 1 Chemistry > Flashcards

Chapter 1 Chemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Atom

A

Consist of a nucleus that has positively charged protons and neutrally charged atoms.
Electrons are located outside the nucleus and are negative.

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2
Q

Molecules

A

Group of 2 or more atoms held by a chemical bond

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3
Q

Electronegativity

A

Ability for atom to attract electrons

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4
Q

Ionic bonds

A

form when one or more electrons are transferred from one atom to the other. The electroengativities are very different and one atom has a strong pull on the electrons compared to the other atom.

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5
Q

Covalent bonds

A

Forms when electrons between atoms are SHARED

Electronegativites are similar

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6
Q

Nonpolar covalent bond

A

Bonds when electrons are shared equally

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7
Q

4 important classes of organic molecules

A

carbohydrates, lipids, proteins, nucleic acids

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8
Q

Carbohydrates

A

SUGAR!! You always forget this

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9
Q

Monosaccharide

A

Simplest for of carb.
Consists of a single sugar molecule (Fructose or Glucose)
Formula (CH2O)n

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10
Q

Disaccharide

A

2 sugar molecules joined by a glycosidic linkage
During the process of joining a water molecule is lost
formula is C12H22O11 not C12H24O12 (due to dehydration reaction)

Glucose + fructose= sucrose
Glucose + galactose = lactose
Glucose+ glucose = maltose

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11
Q

Polysaccharide

A

Series of connected monosaccharides (single sugar molecule)

POLYMER- has repeating units of a monosaccharide

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12
Q

Starch

A

polymer of a-glucose

-Energy storage in PLANTS

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13
Q

Glycogen

A

polymer of a-glucose
differs from starch by polymer branching
-Energy storage in ANIMAL CELLS

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14
Q

Cellulose

A

Polymer of B-glucose molecules

Function: Structural molecule in the walls of PLANTS and major component of wood

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15
Q

Chitin

A

Polymer similar of cellulose
Has B-glucose molecules has NITROGEN-CONTAINING GROUP attached to the ring.
Function: Structural molecule in walls of FUNGUS CELLS and exoskeleton of insects, antropods and mollusks

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16
Q

Lipids

A

Insolubule in water

Soluble in nonpolar substances (ether and chloroform)

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17
Q

3 Major forms of lipids?

A

Triglycerides, Phospholipid, Steriod

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18
Q

Triglyceride

A

Fats and oils
3 fatty acid attached to a glycerol backbone
Fatty acids are hydroharbon (C and H with a carboxyl group -COOH)

Saturated fatty acid- all single bonds
Monosaturated fatty acid- One single bond
Polyunsaturated fatty acid- Multiple double bonds (2 or more)

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19
Q

Phospholipid

A

Has 2 fatty acid chains, glycerol backbone, and a phosphate group (-PO3^2-) with a R group
Function: Structural foundation of cell membrane

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20
Q

Steroids

A

backbone of 4 linked carbon rings (three 6 C and one 5C)

Ex. Cholesterol, hormones, testosterone, estrogen

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21
Q

Categories of Proteins

A
  1. Structural proteins- keratin (hair and horns), collegen (connective tissue), silk (spider webs)
  2. Storage Proteins- casein in milkm ovalbumin in egg whites, zein in corn seeds
  3. Transport proteins- Members of cells that transport materials into and out of cells
  4. Defensive proteins- antibodies that provide protection again foreign substances that enter the bodies of animals
  5. Enzymes- regular the rate of chemical reactions
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22
Q

Amino acid

A

Central carbon bonded to an amino group (-NH2), a carboxyl group (-COOH) and a hydrogen atom, and R

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23
Q

Proteins

A

Proteins are polymers of amino acids that are covalently bonded.
Protein differs by the NUMBER and ARRANGEMENTS of amino acids

24
Q

Peptide bonds

A

bonds located between amino acids to make a protein

25
Q

Polypeptide

A

A chain of amino acid and peptide bonds

26
Q

Structure of Proteins

A

Primary, Secondary, tertiary, quarternary

27
Q

Primary Structure

A

Describes order of amino acids

28
Q

Secondary Structure

A

3D shape due to HYDROGEN BONDING b/w amino and carboxyl groups of aa right next to each other

This makes alpha helix or beta pleated sheets

29
Q

Tertiary Structure

A

Additional 3D shape
Hydrogen bonding between R groups
Ionic bonding between R groups
Hydrophobic effect ( hydrophobic R groups moces away from water)
Disulfide bonds ( sulfur in cysteine bonds to sulfur in another cysteins) -maintains turns of the aa chain

30
Q

Quarternary Structure

A

When 2 or more separate peptide chains interact

Held by hydrogen bonding, interaction among R groups and disulfide bonds

31
Q

DNA

A

Polymer of nucleotides

Consists: nitrogen base, 5 carbon sugar (deoxyribose), phosphate group

32
Q

DNA nucleotides

A

Adenine- double ring (purine)
Thymine- single ring (pyrimidine)
Cytosine- single ring (pyrimidine)
Guanine- double ring (purine)

33
Q

Pyrimidines

A

single ring nitrogen bases

34
Q

Purines

A

Double ring nitrogen bases

35
Q

RNA

A

sugar is ribose
Thymine replaced by uracil
SINGLE STRANDED does not form a double helix like DNA

36
Q

Catabolism

A

Break down of substances

37
Q

Anabolism

A

formation of new products

38
Q

Equilibrium

A

rate of forward equals the rate in the reverse reaction

no net production of reactants or products

39
Q

Enzymes

A

Globular proteins that act as catalyst (activators or accelerators) for metabolic reactions

40
Q

Substrate

A

Substance of substances which enzyme reacts

41
Q

Enzymes characteristics

A
  1. Substrate specific
  2. Unchanged after a reaction and can be reused
  3. Can catalyze both forward and reverse of a reaction
  4. Temperature and pH affects the efficiency - above 104 becomes denatured
  5. Standard suffix is “ase”
42
Q

Induced fit model

A

There is an active site where the reactants readily interact due to shape, polarity or other characteristics. This interaction causes enzyme to change shape which places the substrate molecules into a more favorable position.

43
Q

Cofactor

A

Non protein molecules that assist the enzyme

44
Q

Holoenzyme

A

Union of both cofactor and enzyme

45
Q

Apoenzyme

A

when an enzyme is part of a Holoenzyme

46
Q

Coenzymes

A

organic cofactors that function to donate or accept component of reaction (usually electrons)

47
Q

Inorganic cofactors

A

Metal ions, Fe2+ or Mg2+

48
Q

ATP

A

Adenosine trophosphate

Components: Ribose, adenine and 2 phosphates?

49
Q

Allosteric enzymes

A

have 2 binding sites

  • active site
  • and allosteric site
50
Q

Allosteric activator

A

binds to enzyme and induces the active form

51
Q

Allosteric inhibitor

A

binds to enzyme and induces inactive form

52
Q

Feedback inhibition

A

end product acts as an allosteric INHIBITOR which shuts down one of the enzymes that catalyzes reaction

53
Q

Competitive inhibition

A

Substance that mimics the substrate which inhibits the enzyme since the substance occupies the active site

54
Q

Noncompetitve inhibition

A

Substance inhibits the enzyme by binding to the location NOT at the active site. This changes the shape of the enzyme and stops enzymatic activity

55
Q

Cooperativity

A

enzyme becomes more sensitive to additional substrate after this substrate attaches to the active site

ex. hemoglobins binding activity to o2 increases after the first o2 molecule binds to an active site

Cliffs AP Bio (6 decks)

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