Chapter 3.2- Macromolecules (II) Flashcards

1
Q
  • Macromolecules specialized in storing genetic information
    -Play a role in the direction of the production of proteins and inheritance of an individual
    -Linear unbranched polymers of nucleotides
A

nucleic acids

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2
Q

2 main types of nucleic acids

A

-Deoxyribonucleic acid (DNA)
-Ribonucleic acid (RNA)

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3
Q

What are the nucleotides of nucleic acids made of?

A

-5 carbon sugar
-Phosphate group
-Nitrogenous base

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4
Q

-Contains 5-carbon sugar -deoxyribose
-One less oxygen than RNA sugar ribose
-Forms backbone with phosphate group

A

DNA

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5
Q

Types of nitrogenous bases of DNA

A

-Adenine
-Guanine
-Cytosine
-Thymine

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6
Q

DNA- A always pairs with?

A

T

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7
Q

DNA- G always pairs with

A

C

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8
Q

What are bases held together by?

A

hydrogen bonds

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9
Q

-Contains ribose sugar with one extra oxygen tom
-Single-stranded with only one backbone, not two

A

RNA

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10
Q

Nitrogenous bases of RNA

A

-Adenine
-Guanine
-Cytosine
-Uracil

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11
Q

Which replaces Thymine with Uracil

A

RNA

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12
Q

-Acts as a middleman to convert DNA into specific protein

A

RNA

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13
Q

What makes up 50% of the dry mass of the cell?

A

proteins

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14
Q

Functions of Proteins

A

-Catalysis
-Structure
-Communication
-Transport
-Motility
-Defense
-Recognition
-Regulation

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15
Q

Proteins are unbranched polymers of?

A

amino acids

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16
Q

All 20 amino acids have identical

A

backbone structure

17
Q

The difference in amino acids are determined by

A

R- group

18
Q

linear sequence of covalently bonded amino acids

A

polypeptide

19
Q

one or more polypeptides folded into a functional 3D conformation

A

protein

20
Q

Levels of Protein Structure

A

-Primary
-Secondary
-Tertiary
-Quaternary

21
Q

Two cysteine residues come close together to form

A

Disulfide Bond (bridge)

22
Q

What environmental conditions affect protein shape?

A

-Temp
-Ionic Strength
-pH

23
Q

What can misfolded proteins cause?
(due to mutations or disruptions of normal folding processes)

A

clinical diseases

24
Q

Why is glu to val change significant?

A

-nonconservative amino acid change
-changes overall protein structure