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Bio of Food and Nutrition > Chapter 5 - Proteins > Flashcards

Chapter 5 - Proteins Flashcards

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1
Q

Protos

A

“primary importance”
-protos wine
-protoss game
-protos wagen (german car company)

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2
Q

Protein

A

-part of every cell and a source of energy in your body
-builds and repairs tissues (like skin and muscle)
-makes vital substances as antibodies, insulin
-found in: hard boiled eggs, hummus, edamame, milk, tuna, nuts, chickpeas, etc
-complex macromolecules from combination of 20 types of amino acids: basic building block of protein

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3
Q

Essential Amino Acids

A

-8/20 amino acids are essential, and found in food because can’t be made by the body
-indispensable

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4
Q

Nonessential Amino Acids

A

-12/20 amino acids are nonessential, and can be made by the human body (with enough C, N, H, O
-dispensable

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5
Q

Complete Proteins

A

proteins with only essential amino acids

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6
Q

Incomplete Proteins

A

missing at least 1 essential amino acid

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7
Q

Methionine

A

essential AA
-coded by codon AUG, called start codon
-1st AA used to build protein chain

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8
Q

Central Dogma Process

A

process to synthesize AA from DNA (info for proteins)
1.) Replicate DNA (requires deoxyribose, N base pair, Phosphate G)
2.) Transcription: make DNA into RNA
3.) Translation: make RNA into AA

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9
Q

Hemoglobin

A

protein
-bonds with and carries ozygen molecules

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10
Q

Functions of Body Proteins

A

-enzymes: speeds up chemical reaction
-hormones: chemical messenger
-antibody: made to protect from foreign substances
-fluid balance: pumps molecules across cell membranes and attracts water
-transport key substances (CO2, vitamins, minerals) to target cells in body
-acid-base balance
-structural and mechanical

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11
Q

AA Structure

A

-20 AAs commonly found in proteins, each with a different R group that determines chemical nature
-grouped by polarity or charge

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12
Q

1st AA Structure Grouping

A

Nonpolar, Aliphatic R group

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13
Q

2nd AA Structure Grouping

A

Polar, Noncharged - can be both because it is easily charged

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14
Q

3rd AA Structure Grouping

A

Positively Charged

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15
Q

4th AA Structure Grouping

A

Negatively Charged

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16
Q

5th AA Structure Grouping

A

Nonpolar Aromatic (ring structure)

17
Q

Which AA grouping is Hydrophobic?

A

1 and 5

18
Q

Amphipathic

A

both polar and nonpolar

19
Q

Amino Acids to Protein

A

-AAs link is specific sequences to form standards of proteins (peptides) up to 100 of AAs long
-AA joined to the next with a peptide bond
-2 AA = dipeptide
-3 AA = tripeptide
-4-10 AA = oligopeptide
-> 10 AA = polypeptide
-Peptide bond formation done with dehydration synthesis - carboxyl group bonds with amino group

20
Q

Aldose

A

Carboxyl Group at the end

21
Q

Ketose

A

Carboxyl Group in the middle

22
Q

Primary Polypeptides

A

a long chain of polypeptides only
-no function

23
Q

Folding

A

Polypeptides need a specific structure to function
-creates 3D shape which determines function and interaction with other molecules

24
Q

Secondary Polypeptides

A

alpha helix or beta sheet form because of Hydrogen bonding between a Carbonyl and Amino Group
-no function!

25
Q

Tertiary Polypeptides

A

-AA helices/sheets are folded over eachother to form 3D folding pattern
-variety of chemical interactions determine proteins’ tertiary structure: hydrophobic, ionic bond, hydrogen bond, disulfide linkages
-some function

26
Q

Quaternary Polypeptides

A

2+ proteins in T structure are associated with each other (2+ tertiary structures)
-all of these proteins are functional

27
Q

Denaturation

A

-alteration in 3D structure, causes unfolded polypeptide chain that usually lacks biological activity (destabilizing proteins shape)
-usually caused by acids, bases, enzymes, heat, and others
-can be reversed (structure reformed) as renaturation

28
Q

Mutation

A

changes in DNA - AA

29
Q

Enzyme and Substrate Example

A

Amylase - Amylose
Lipid - Lipase
-Protein - Protease

30
Q

Sickle Cell Anemia

A

-change in the nucleotide sequence of gene’s coding – diff AA is added with changes in protein structure and function
-hemoglobin beta chain in protein structure and function
-dramatically decreases life expectancy
-single AA substitution leads to SCA
-normal hemoglobin: AA at position 7 = glutamate
-SC hemoglobin: valine replaces glutamate which forms into long fibers that distort into disc-shaped red blood cells –> giving them sickle shape which clogs blood vessels and can lead to : breathlessness, dizziness, headaches, abdominal pain

31
Q

Enzymes

A

proteins that catalyze reactions in our body (like dehydration synthesis and hydrolysis)
-work like lock and key: can build or break molecules down; not all keys work on any lock

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