Module 4 - Proteins Flashcards

1
Q

The central atom

A

Carbon

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2
Q

Carbon can be in a form of a

A

Ring or a chain

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3
Q

Carbon has how many valence electrons

A

4 valence electrons

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4
Q

Carbons are highly stable T OR F

A

True

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5
Q

Main element used in biomolecules

A

Carbon

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6
Q

Single chemical unit that creates polymers

A

Monomers

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7
Q

Creation of polymers in via

A

Dehydration synthesis

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8
Q

Biomolecule units that can be broken down into monomers

A

Polymers

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9
Q

Bread down into monomers is via

A

Hydrolysis

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10
Q

A biochemical process forms a larger molecule by

A

removal of water

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11
Q

Removal of a water molecule

A

Dehydration reaction

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12
Q

Dehydration reaction forms a

A

Larger molecule

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13
Q

The reverse process of dehydration reaction

A

Hydrolysis reaction

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14
Q

The break down of larger molecule to smaller molecule is by

A

Adding a water molecule

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15
Q

Hydrolysis is essential for

A
  1. Digestion
  2. Metabolism
  3. Nutrient absorption
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16
Q

Found and used by all living

A

Biomolecules

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17
Q

4 classifications of biomolecules

A
  1. Proteins
  2. Carbohydrates
  3. Nucleic Acid
  4. Lipids
18
Q

How can we say that a molecule is organic

A

Includes a carbon atom

19
Q

Most abundant macromolecule

20
Q

Building block of proteins

A

Amino acids

21
Q

Protein structure of an amino acid

A

central carbon atom bonded to an amino group (NH₂), a carboxyl group (COOH), a hydrogen atom (H), and a side chain (R group)

22
Q

Guves an amino acid its unique property

23
Q

Links the amino acids together to form protein

A

Peptide bond

24
Q

Where is peptide bond formed

A

between the carboxyl group of one amino acid and the amino group of another amino acid.

25
Q

Linear sequence of amino acids in a peptide chain

A

Primary structure

26
Q

Folding patterns of a polypeptide chain such as alpha helix and beta sheet

A

Secondary structure

27
Q

Overall 3D shape of a protein determined by interactions between amino acid side chains

A

Tertiary structure

28
Q

Arrangement of multiple polypeptide chains in a protein complex

A

Quaternary structure

29
Q

What are the intermolecular forces used in stabilizing protein structures

A
  1. Hydrogen bonds
  2. Ionic or salt bridges
  3. Van der Waals forces
  4. Disulfide bonds
30
Q

What does hydrogen bond stabilize

A

Secondary structures like alpha helices and beta sheets

31
Q

What happens through ionic interactions in stabilizing protein structure

A

Charged amino acid side chains can interact with each other

32
Q

What does Van der Waals forces stabilize

A

Tertiary and quaternary structures of protein

33
Q

Disulfide bonds can form between

A

Sulfur atoms of two cysteine residues

34
Q

Function of protein: catalyze chemical reactions to sped up

A

enzyme or catalsts

35
Q

Function of protein: muscle movement like actin or myosin

36
Q

Function of protein: protect the body from pathogens

37
Q

Function of protein: regulate gene expression and cellular process

A

Regulation

38
Q

Function of protein: transport molecules across cell membranes

39
Q

Function of protein: provide structural support to tissues

40
Q

Function of protein: store nutrients and amino acids