Lecture 5: The Molecules Of Life Flashcards

1
Q

Enzymes

A

Specialized macromolecules that speed up chemical reactions

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2
Q

Dehydration reaction

A

2 monomers bond together through loss of a water molecule

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3
Q

Hydrolysis

A

Polymers disassembled to monomers through addition of a water molecule

Hydrogen from water attaching to one monomer and hydroxyl group attaching to other

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4
Q

Monosaccharides

A

Simple sugar

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5
Q

Disaccharide

A

Consists of 2 monosaccharides joined by a glycosidic linkage

Covalent bond formed between 2 monosaccharides by a dehydration reaction

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6
Q

Polysaccharides

A

Polymers of many sugars joined by glycosidic linkages via dehydration synthesis

Ex. Starch, glycogen, cellulose

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7
Q

Starch

A

Storage form of glucose in plants

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8
Q

Glycogen

A

Storage form of glucose in animals

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9
Q

Cellulose

A

Contribute fiber

Like starch, cellulose is a polymer of glucose, but glycosidic linkages differ

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10
Q

The difference between starch and cellulose is based on

A

2 ring forms for glucose: alpha(α) and beta (β)

Starch is alpha configured and is largely helical

Cellulose molecules are beta configured and straight and unbranched

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11
Q

Enzymes that digest starch by hydrolyzing alpha linkages

A

Can’t hydrolyze beta linkages in cellulose

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12
Q

Cellulose in human food passes through the digestive tract as

A

“Insoluble fiber”

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13
Q

Fats

A

Constructed from 2 types of smaller molecules: glycerol and fatty acids

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14
Q

Glycerol is

A

3 carbon alcohol with a hydroxyl group attached to each carbon

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15
Q

Fatty acid is

A

One Carboxyl group attached to a long carbon skeleton

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16
Q

Fats separate from water because

A

Water molecules hydrogen-bond to each other exclude fats

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17
Q

Nonpolar C-H bonds in hydrocarbon chains of acids are

A

Hydrophobic

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18
Q

Saturated fatty acids

A

No double bonds between C atoms of chain

Allows fat molecules to pack together tightly (butter- solid at room temperature)

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19
Q

Unsaturated fatty acids

A

1 or more double bonds between C atoms

Kinks of double bonds prevent molecules from packing closely together and can’t solidify (olive oil-liquid at room temperature)

20
Q

Hydrogenation

A

Process of converting unsaturated fats to saturated fats by adding hydrogen

Allows them to solidify

21
Q

Trans fats may contribute

A

More than saturated fats to cardiovascular disease

22
Q

Phospholipids structure

A

Amphipathic:

2 long hydrocarbon tails (fatty acids)- Hydrophobic (nonpolar)

1 glycerol molecule attached to phosphate group- Hydrophilic (polar)

23
Q

In water, phospholipids self-assemble into

A

A bilateral or micelles

-hydrophilic heads on outside
-hydrophobic tails point towards interior

24
Q

Protiens

A

Polypeptides are unbranched polymers built from the same set of 20 amino acids (monomers)

25
Q

R group

A

Variable side chain of 1 or more atoms that identifies a specific amino acid

Contributes to overall shape and function of proteins

26
Q

Amino acids join by

A

Dehydration synthesis

27
Q

Peptide bond formation

A

Covalent bond between Carboxyl group of 1 amino acid and amino group of another

28
Q

Polypeptide

A

Polymers of many amino acids linked by peptide bonds

29
Q

Primary protein structure is determined by

A
  1. Number of amino acids in chain
  2. Specific sequence of amino acids
30
Q

Secondary protein structure

A

Consists of coils and folds in polypeptide chain

Result from H-bonding between atoms within polypeptide chain

31
Q

Alpha helix

A

Simple spiral/coil

32
Q

Beta sheet

A

Flat pleated sheet/parallel

33
Q

Tertiary protein structure

A

Overall shape of a polypeptide, results from interactions between R groups (side chains), rather than interactions between backbone constituents

34
Q

Tertiary protein structure contributing interactions:

A

H-bonds, ionic bonds, hydrophobic interactions, van der Waals forces, disulfide bridges

35
Q

H-bonds

A

Between polar side chains

36
Q

Ionic bonds

A

Between charged side chains

37
Q

Hydrophobic interactions

A

Nonpolar side chains end up in clusters at core of protein, out of contact with water

38
Q

Van der Waals forces

A

Helps hold nonpolar side chains together

39
Q

Disulfide bridges

A

Covalent disulfide bonds between 2 cysteine monomers which have Sulfhydryl groups as side chains

Reinforce protein structure

40
Q

Denaturation

A

Loss of a protein’s native structure

A desaturated protein is biologically inactive

Extremely high fevers can be fatal- proteins in blood tend to denature at very high body temperatures

41
Q

Nucleic acids structure

A

DNA and RNA consist of long chains of nucleotides(monomers), which contain:
1. Pentose (5-C) sugar (DNA or RNA)
2. Phosphate group
3. Nitrogenous Base (A, G, T, C, or U)

42
Q

Nucleoside

A

Nitrogenous base + sugar

43
Q

Purine bases

A

Adenine(A) and guanine (G)

6 membered ring fused to a 5 membered ring

44
Q

Pyrimidine bases

A

Cytosine (C), thymine (T), Uracil (U)

Single 6 membered ring

45
Q

Nucleotides are linked together by

A

A phosphodiester linkage to build a polynucleotide

46
Q

Phosphodiester linkage

A

Phosphate group that links sugars of nucleotides

These links create a backbone of sugar-phosphate units with nitrogenous bases as appendages