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Biology 1406 - 01M > Topic 3 > Flashcards

Topic 3 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

organic chemistry

A

Organic chemistry is the study of the structure, properties, composition, reactions, and preparation of carbon-containing compounds.

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2
Q

hydrophilic

A

“Water loving”

a phospholipid has a polar head which is hydrophilic and they point outwards

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3
Q

hydrophobic

A

“Water hating”

a phospholipid has a nonpolar tail which is hydrophobic and they point inwards towards each other

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4
Q

macromolecules

A

There are four classes: carbohydrates, proteins, lipids, and nucleic acids

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5
Q

polymer

A

are long molecules built by linking together many smaller molecules, that are similar chemical subunits called monomers. Ex. starch, polypeptide chains, triglycerides, DNA

are formed via dehydration synthesis, and broken down via hydrolysis

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6
Q

monomers

A

are smaller individual subunits of polymers, which make up carbohydrates, lipids, proteins, nucleic acid. Ex. monosaccharides, nucleotides, amino acids, fatty acids

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7
Q

enzymes

A

globular proteins that act as biological catalysts

functional enzymes, referred to as holoenzymes, consist of two parts
Apoenzyme (protein portion) & Cofactor (metal ion) or coenzyme (organic molecule, often a vitamin)

Act on a very specific substrate & Names usually end in –ase and are often named for the reaction they catalyze

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8
Q

dehydration synthesis reaction

A

the process of combining monomers to form polymers by removing water. It builds molecules and requires energy. Examples of this in organic molecules would be amino acids combining to form proteins, monosaccharides combining to form complex sugars, nucleic acids forming from nucleotides, & fatty acids becoming complex fats.

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9
Q

hydrolysis

A

the decomposition of molecules into its components by adding water (the bond between two monomers is broken). It breaks down molecules and releases energy. Examples of this with organic molecules are when complex carbs break down into simple sugars, lipids into fatty acids and glycerol, nucleic acids to nucleotides, proteins into amino acids.

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10
Q

carbohydrates (function, fundamental structure, polymer and monomer state)

A

used for quick energy storage

C, H, O - Ch2O

the monomer is a monosaccharide

the polymer is a polysaccharide

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11
Q

monosaccharides

A

monomer of carbohydrates

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12
Q

disaccharide

A

formed by linking two monomers, used especially in carbohydrates to transport glucose to tissues.

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13
Q

polysaccharides

A

polymer of carbohydrates

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14
Q

starch

A

a polymer of carbohydrates

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15
Q

glycogen

A

a polymer of carbohydrates

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16
Q

cellulose

A

a polymer of carbohydrates

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17
Q

lipids (function, fundamental structure, polymer and monomer state)

A

The main characteristic that all lipids have in common is that they do not dissolve in water.

can be storage fats, oil, or waxes

very high proportion of nonpolar carbon hydrogen (C-H) bonds.

the monomer is a fatty acid chain/glycerol

the polymer is triglycerides

9 kcal/g for lipids, compared to 4kcal/g for carbohydrate

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18
Q

fats

A

the ratio of energy-stored in fats is twice that of carbohydrates

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19
Q

fatty acids

A

a monomer of lipids

Fatty acid chains can be saturated, unsaturated or polyunsaturated.

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20
Q

glycerol

A

a monomer of lipids

21
Q

triglycerol

A

a common fat/storage molecule, that contains three fatty acids, and a glycerol backbone.

22
Q

saturated fatty acid

A

a fat molecule in which all the internal carbon atoms contain the maximum number of hydrogens atoms

23
Q

unsaturated fatty acid

A

a fat molecule in which one or more of the fatty acids contain fewer than the maximum number of hydrogens attached to their carbons

24
Q

phospholipid

A

one of the most important molecules of the cell, because they form the core of all biological membranes

Composed of the: Glycerol, Fatty acid chains, and a phosphate group

allows it to have a Polar “Head” (hydrophilic), and a nonpolar “tail” (hydrophobic)

Phospholipid bilayer – composed of 2 layers of phospholipids, form the plasma membrane of cells, separating the extracellular and intracellular spaces.

25
Q

steroids (lipid molecule)

A

any of a class of natural or synthetic organic compounds characterized by a molecular structure of 17 carbon atoms arranged in four rings (estrogen and testosterone are considered steroids), amphipathic

26
Q

cholesterol

A

a sterol that is essential to life and fulfills several biological functions…

  • Primary component of the membrane that surrounds each cell
  • starting ingredient for the synthesis of bile acids, steroid hormones, and vitamin D

A STEROID WITH FOUR FUSED CARBON RINGS

27
Q

catalysts

A

regulate and increase the speed of chemical reactions without getting used up in the process & Lower the energy needed to initiate a chemical reaction

28
Q

polypeptide

A

polymer of amino acids joined together by peptide bonds

29
Q

protein (function, fundamental structure, polymer and monomer state)

A

have multitudinous functions in an organism, including Enzyme catalysis, Defence, Transport, Support, Motion, Regulation, Storage

made from 20 types of amino acids

have an amine group and an acid group

C, H, O, N, and sometimes S and P

the monomer is amino acids

the polymer is polypeptide chains

30
Q

amino acid

A

have an amine group and an acid group

held together by peptide bonds (covalent)

can act as either an acid or a base

Differ by which of 20 different “R groups” is present

31
Q

peptide bond

A

covalent bonds that hold amino acids together

32
Q

the four types of protein structures

A

primary, secondary, tertiary, quaternary

33
Q

primary structure

A

simply a linear sequence of amino acids (Polypeptide chain). It is the simplest level.

34
Q

secondary structure (alpha helix, beta-pleated sheet)

A

how primary amino acids interact with each other (folding or coiling) (held together by hydrogen bonds)

Alpha (α) helix coils resemble a spring
Beta (β) pleated sheets resemble accordion ribbons

35
Q

tertiary structure

A

how secondary structures interact. (Same Polypeptide chain)

36
Q

quaternary structure

A

how 2 or more different polypeptides interact with each other

37
Q

denaturation

A

globular proteins unfold and lose their functional 3-D shape. Fibrous proteins are more stable & active sites become deactivated

Can be caused by decreased pH (increased acidity) or increased temperature. Usually reversible if normal conditions restored. Irreversible if changes are extreme

38
Q

nucleic acids (function, fundamental structure, polymer and monomer state)

A

the largest of the organic molecules and they store and express an organism’s genetic information

C, H, O, N, P

major classes are DNA & RNA

the monomer is nucleotides

a polymer is Deoxyribonucleic acid

39
Q

nucleotide

A

Composed of nitrogen base, a pentose sugar, and a phosphate group

40
Q

deoxyribonucleic acid (DNA)

A

Double-stranded helical molecule (double helix) located in cell nucleus

holds the genetic blueprint for the synthesis of all proteins

Bonding of nitrogen base from strand to opposite strand is very specific

Follows complementary base-pairing rules:
Adenine always pairs with Thymine
Guanine always pairs with Cytosine

Nucleotides for DNA contain a deoxyribose sugar, phosphate group, and one of four nitrogen bases:
Purines: adenine (A), guanine (G)
Pyrimidines: cytosine (C) and thymine (T)

41
Q

Ribonucleic acid (RNA)

A

RNA links DNA to protein synthesis and is slightly different from DNA

Single-stranded linear molecule is active mostly outside nucleus

Contains a ribose sugar (not deoxyribose)

Thymine is replaced with uracil

Three varieties of RNA carry out the DNA orders for protein synthesis: Messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA)

42
Q

What particular element, and their molecules are considered to be organic compounds, and why?

A

Carbon because its unique ability to form strong covalent bonds with other elements, including itself. This allows carbon to form a huge variety of compounds with different structures and functions

43
Q

Understand why functional groups affect the properties of macromolecules.

A

A functional group is a molecular group attached to a hydrocarbon that confers chemical properties or reactivities. Examples include hydroxyl (– OH), carboxylic acid (– COOH) and amino groups (– NH2).

display consistent “function” (properties and reactivity) regardless of the exact molecule they are found in

play a crucial role in determining the properties of macromolecules, including their structure, solubility, reactivity, and polarity.

44
Q

An acid with a pH of 3 is how many times more acidic than an acid with a pH of 6?

A

1000

45
Q

What ratio are carbon, hydrogen, and oxygen are typically found in carbohydrates ?

A

1:2:1

46
Q

The tendency of an atom to pull electrons toward itself is referred to as its ____?

A

electronegativity

47
Q

The flow of genetic information in a cell, proceeds in what direction?

A

DNA -> RNA -> Amino acids

48
Q

A lipid would be considered unsaturated because?

A

the presence of double bonds

49
Q

ATP Structure

A

the nitrogenous base, adenine; the sugar, ribose; and a chain of three phosphate

Biology 1406 - 01M (19 decks)

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