Macromolecules (Exam 2) Flashcards

(40 cards)

1
Q

Define inorganic molecule in terms of composition

A

Lack carbon, all other molecules

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2
Q

Define organic molecule in terms of composition.

A

Molecules that contain carbon
Most are a component of living organisms
Biological macromolecules (biomolecules) are a subset

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3
Q

What common elements are found in proteins

A

CHON +/- sulfur

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4
Q

What common elements are found in carbohydrates

A

CHO

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5
Q

What common elements are found in lipids

A

Carbon, hydrogen, and oxygen

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6
Q

Describe at least 3 common functions of lipids.

A

Stored nutrients/energy
Cellular membrane components
Hormones
Cushioning
Insulation

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7
Q

What are the four classes of lipids?

A

Triglycerides
Phospholipids
Steroids
Eicosanoids

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8
Q

Which lipid is considered to be “dietary fats”?

A

Triglycerides

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9
Q

Examples of unsaturated fats

A

Fish
Some oils- olive, peanut, canola, corn
Nuts, seeds, avocados
“Liquids”

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10
Q

Examples of saturated fats

A

Fatty meats
Dairy products- cream, whole milk, cheese, etc.
Processed foods
“Solids”

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11
Q

Which fat is considered to be more healthy for you and why?

A
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12
Q

Define lipolysis

A
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13
Q

Define lipogenesis

A
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14
Q

Describe the structure of phospholipid

A

One end is glycerol, phosphate, and organic group (polar): known as the hydrophilic head
One end is fatty acids (non-polar): known as hydrophobic tails

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15
Q

Describe the structure of steroid

A

Composed of hydrocarbons arranged in a multi-ringed structure
Differ in the side chains extending from their rings

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16
Q

Describe the structure of eicosanoid

A

Modified 20-carbon fatty acids synthesized from arachidonic acid, membrane component

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17
Q

Describe the structure of triglyceride

A

Formed from a glycerol molecule and three fatty acids

18
Q

Which class of lipid is found commonly in cell membrane structure?

A

Phospholipids

19
Q

Give two examples of lipid steroids.

A

cholesterol
hormones
bile
salts

20
Q

Describe two functions of eicosanoids.

A

Inflammatory pathways (including pain response)
Immune response

21
Q

Give three examples of monosaccharides. Which monosaccharides is the most common in the body?

A

Glucose, galactose, fructose
Glucose

22
Q

Give two examples of disaccharides.

A

Sucrose (table sugar), lactose (milk sugar), maltose (malt sugar)

23
Q

Define a polysaccharide. Which polysaccharide is the most common in the body?

A

Three or more carbs bonded together
glycogen

24
Q

How do we gain energy from carbohydrates?

25
Which monosaccharide is considered to be “blood sugar”?
Glucose
26
Describe the relationship between glucose and glycogen.
Glucose is converted to glycogen for short-term storage
27
How does carb-loading work? What is the purpose of carb-loading?
28
Give two examples of nucleic aids.
Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA) Adenosine triphosphate (ATP)
29
Which nucleotides are found within DNA? RNA?
Adenine (A) - DNA and RNA Thymine (T) - DNA only Uracil (U) - RNA only Guanine (G) - DNA and RNA Cytosine (C) - DNA and RNA
30
Describe the components of a nucleotide.
Pentose sugar Phosphate group Nitrogenous base
31
Which nucleotides bind together in DNA? What kind of bonds are found between nucleotides?
Adenine and Thymine Guanine and Cytosine
32
What kind of bonds are found between nucleotides?
33
Which nitrogenous bases are found in RNA?
34
What is the structure of ATP? What is ATP used for?
Adenine and Uracil Guanine and Cytosine
35
Describe at least 4 specific functions of proteins.
36
What is the general structure of an amino acid?
37
How many amino acids are there? Of those, how many are considered to be “essential”? What does this mean?
20 naturally existing amino acids 9 are essential
38
Distinguish between the primary, secondary, and tertiary structure of a protein. Of these, which is considered to the be “final” shape for most proteins?
Primary: a linear sequence of amino acids Secondary: structural patterns due to hydrogen bonds Tertiary: final 3-D shape for most proteins Tertiary is the final shape for most proteins
39
What is an example of a quaternary protein?
Hemoglobin
40
Define the term protein denaturation. What factors may result in protein denaturation?
Disruption of protein shape Disturbs protein activity → loss of function Usually irreversible