Proteins Flashcards

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1
Q

What atoms do all proteins contain

A
  1. Carbon
  2. Hydrogen
  3. Oxygen
  4. Nitrogen
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2
Q

What atom do MOST proteins contain

A

Sulfur

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3
Q

What atoms do SOME proteins contain

A
  1. Zinc
  2. Copper
  3. Iron
  4. Phosphorus
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4
Q

How many calories per gram do proteins contain and what is the nitrogen content

A

4 calories per gram

16% nitrogen

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5
Q

What are the four basic parts of amino acids

A
  1. Side Chain (R group)
  2. Amine group
  3. Hydrogen atom
  4. Carboxyl group
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6
Q

how long can amino acids be stored in the body and how often do they need to be supplied

A
  1. They are not stored in the body

2. Need to be supplied in the diet daily

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7
Q

what bond joins amino acids

A

peptide bonds

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8
Q

what is produced when two amino acids joined

A

dipeptide bonds and water

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9
Q

Describe the primary structure of proteins

A
  1. linear arrangement of amino acids

2. a sequence

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10
Q
  1. How many structures are in the secondary structure
  2. What are these structures?
  3. What dictates which is formed?
A
  1. 3
  2. Beta pleated sheets, alpha helix, random coil
  3. the hydrogen bonds and pattern of backbone
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11
Q

What are the 2 tertiary structures and their functions

A
  1. Fibrous: structure, they are elongated molecules formed from repeating alpha helixes or beta pleated sheets and they are INSOLUBLE
  2. Globular: transport, hydrophobic amino acids residues and hydrophilic residues, straight runs of secondary structure
    SOLUBLE
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12
Q

What makes up the quaternary structure

A

more than 2 tertiary structures

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13
Q

how does protein stability compare to carbs and lipids?

A

proteins change drastically when exposed to heat, air, osmotic pressure, or ph while carbs and lipids don’t change that much

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14
Q

Define protein confirmation and denaturation

A

Denaturation: unfolding of protein molecule, changes shape without changing primary structure

Confirmation: normal structure and activity of protein

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15
Q

2 physical denaturations of proteins and examples

A
  1. heat: heating egg which then cannot go back to original form
  2. air: when exposed to air proteins change and cannot return to original state
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16
Q

2 ways proteins are chemically denatured

A
  1. pH: pickle food

2. osmotic pressure: using salt to change structure of protein

17
Q

define reversible and irreversible protein denaturation

A
  1. Reversible: protein can return to its original confirmation and biological activity
  2. irreversible: protein cannot go back to original state or activity
18
Q

Define Complete and Incomplete protein quality and give sources of each

A
  1. Complete: contains all essential amino acids in approximately the right proportions EX: meat and fish
  2. Incomplete: lacks certain amino acids
    EX: nuts, seeds
19
Q

Define Protein complementation

A

completing the amino acid pattern by consuming complementing proteins, one contains what the other is lacking

BEANS AND RICE

20
Q

5 functions of protein in food

A
  1. water binding
  2. reduction
  3. hydrolysis
  4. texturize
  5. emulsify
21
Q

what is protein hydrolysis and what is the necessary input

A
  1. breaking down the peptide bond

2. water