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
Linear sequence of amino acids in a peptide chain
Primary structure
26
Folding patterns of a polypeptide chain such as alpha helix and beta sheet
Secondary structure
27
Overall 3D shape of a protein determined by interactions between amino acid side chains
Tertiary structure
28
Arrangement of multiple polypeptide chains in a protein complex
Quaternary structure
29
What are the intermolecular forces used in stabilizing protein structures
1. Hydrogen bonds 2. Ionic or salt bridges 3. Van der Waals forces 4. Disulfide bonds
30
What does hydrogen bond stabilize
Secondary structures like alpha helices and beta sheets
31
What happens through ionic interactions in stabilizing protein structure
Charged amino acid side chains can interact with each other
32
What does Van der Waals forces stabilize
Tertiary and quaternary structures of protein
33
Disulfide bonds can form between
Sulfur atoms of two cysteine residues
34
Function of protein: catalyze chemical reactions to sped up
enzyme or catalsts
35
Function of protein: muscle movement like actin or myosin
Motion
36
Function of protein: protect the body from pathogens
Defense
37
Function of protein: regulate gene expression and cellular process
Regulation
38
Function of protein: transport molecules across cell membranes
Transport
39
Function of protein: provide structural support to tissues
Support
40
Function of protein: store nutrients and amino acids
Storage