Biological Macromolecules (Chapter 3) Flashcards

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1
Q

Macromolecules

A

Large polymers that synthesized by linking individual monomers (small molecules with similar chemical subunits)

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2
Q

Polymers are formed by?

A

Dehydration synthesis, which is the formation of large molecules by the removal of water

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3
Q

Polymers are broken down by?

A

Hydrolysis, which is the breakdown of large molecules by the addition of water

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4
Q

Carbohydrates

A
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5
Q

Nucleotides

A

-They are composed of a ribose or deoxyribose sugar, a phosphate group, and a nitrogen-containing base.
-Connected by phosphodiester bonds

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6
Q

Deoxyribonucleic Acid and Ribonucleic Acid

A

DNA encodes the information for the amino acid sequence of proteins
-Normally double stranded

Ribonucleic Acid is simply a “carbon copy” of DNA that acts as an intermediate between DNA and the ribosomes that build proteins.
-Normally single stranded

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7
Q

Proteins

A

They are enzymatic catalysis of chemical reactions.
-Transport
-Support
-Motion
-Regulation
-Storage

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8
Q

Amino Acids

A

There are 20 different amino acids that are encoded by eukaryotic genetic code.

They are joined by dehydration synthesis to form peptide bonds.

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9
Q

Conformation

A

The shape of a protein determines its function. Any change in conformation translates into either a gain or loss of function.

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10
Q

What are the 4 levels of protein structure?

A
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
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11
Q

Primary Structure & Secondary Structure

A
  1. The sequence of amino acids
  2. The interaction of groups in the peptide backbone.
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12
Q

Tertiary structure & Quaternary Structure

A
  1. The final folded shape of a globular protein. It is the final level of structure for proteins consisting of only a single polypeptide chain.
  2. The arrangement of individual chains (subunits) in a protein with 2 or more polypeptide chains.
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13
Q

Motifs and Domains

A

Motifs are small common elements of secondary structure seen in many polypeptides.

Domains are functional units within a larger structure.

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14
Q

Chaperones

A

Chaperone proteins (called chaperoning) help protein fold correctly by preventing polypeptide aggregation, and by providing an environment that promotes the ideal folding pattern.

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15
Q

Protein loss of structure and function due to changes in pH, temperature, and/or iconic concentration of solutions is called

A

Denaturation

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16
Q

Lipids

A

-Are loosely defined as molecules that are insoluble in water
-They have a high proportion of non polar C-H bonds that cause them to be hydrophobic.

17
Q

Most fats and oils are

A

Triglycerides
-Triglycerides are composed of 1 glycerol attached to 3 fatty acids by dehydration synthesis.

18
Q

Fatty acid chains may also be

A

Saturated or unsaturated.

19
Q

Saturated means

A

No double bond between carbon atoms, and higher melting point

20
Q

Unsaturated means

A

1 or more double bonds, and low melting point

21
Q

Trans-fats, despite being unsaturated, have a structure that resembles that of

A

Saturated fats

22
Q

Phospholipids are composed of glycerol molecules attached to

A

-Two fatty acids (nonpolar “tails”), and a phosphate group (polar “head”)

23
Q

Amphipathic molecules placed in an aqueous environment spontaneously orient their polar (hydrophilic) head toward the outside and non polar (hydrophobic) tails toward each other, thereby forming

A

Micelles

24
Q

What is Sucrose composed of?

A

Glucose + Fructose