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Biology > Macromolecules > Flashcards

Macromolecules Flashcards

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1
Q

Why are phospholipids different than lipids?

A

They have 2 fatty acid tails

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2
Q

What does Amphiphilic/amphipathic mean?

A

Molecules with hydrophobic and hydrophilic parts

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3
Q

Types of lipids?

A
  1. Steroids
  2. Cholesteral
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4
Q

What is the “bad” cholesterol and why?

A

LDL
It accumulates in the bloodstream due to more fat in them and can cause blockages

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5
Q

What is the “good” cholesterol and why?

A

HDL

Travels through our blood and helps bring cholesterol to our livers for processing, which removes it from the bloodstream

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6
Q

What do all functional groups depend on?

A

Proteins

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7
Q

What are functional groups linked by?

A

Alpha carbons

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8
Q

What are R groups?

A

Provide each amino acid with specific properties (functional group)

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9
Q

What are proteins?

A

One or more polypeptides working together

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9
Q

What types of amino acids can we not make and must get from our food?

A

Essential amino acids

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10
Q

Where do we get most of our amino acids from?

A

Metabolism

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11
Q

What are polypeptides?

A

Strings of amino acids

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11
Q

What are amino acids linked by?

A

Dehydration reactions. The carboxyl group is linked to the amino group via a peptide bond

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12
Q

Describe the ends of a polymer

A

One end of the polymer starts with an amino group (N-terminus), the other ends with a carboxyl group (C-terminus)

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13
Q

Do the amino and carboxyl groups attached to the alpha carbon in linked amino acids have a charge?

A

No!

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14
Q

What determines the way a polypeptide folds?

A

Once amino acids are made, they interact with water in the cytoplasm, as well as each other which causes it to fold

15
Q

What is the folding of a polypeptide dependent on?

A

The sequence of the amino acid, interactions of the R groups, and hydrogen bonding

16
Q

What are the 4 levels of structure of a protein?

A

1.Primary structure
2.Secondary structure
3.Tertiary structure
4.Quaternary structure

17
Q

What is a primary structure?

A

The sequence of the amino acids in the polypeptide chain

18
Q

What is a tertiary structure?

A

The 3D shape of a single polypeptide

19
Q

What is a secondary structure?

A

The coils and fold of the proteins overall shape

20
Q

What is a quaternary structure?

A

The stable, formation of two or more polypeptides

21
Q

What is the definition of DNA?

A

Deoxyribonucleic acid: a polymer of nucleotides that stores genetic information

22
Q

Example of how can changes in primary sequence have big impacts at all levels of structure?

A

Sickle-cell anemia is caused by a substitution of valine for glutamic acid

Causes deformation of disk shape into a crescent moon

Results in the blood cell unable to bind and carry oxygen

Can also cause clogs in the blood vessels

23
Q

What is the definition of RNA?

A

Ribonucleic acid: a polymer of nucleotides that carries the instructions for protein making

24
Q

What is the definition of ribosomes?

A

Molecules of protein and rRNA that translates the mRNA strand into specific amino acids which form polypeptides and proteins

25
Q

Definition of gene expression?

A

The process of transcribing DNA into RNA and translating that into a protein

26
Q

What are the monomers of nucleic acids?

A

Nucleosides- sugar + nitrogenous base

Nucleotides- sugar + carbon base

27
Q

What are nitrogenous bases?

A

Rings that have nitrogen atoms and take up H+

ex. Pyrimidine (Cysteine, Thymine, Uracil)
Purine (Adedine, Guanine)

28
Q

What are the monomers of DNA/RNA

A

Nucleotides

29
Q

A always interacts with? How many bonds?

A

T - 2 H bonds

30
Q

C always interacts with? How many bonds?

A

G- 3 H bonds

31
Q

What is PCR? (polymerase chain reaction)

A

A technique to amplify thousands of copies of a specific piece of DNA that we’re interested in

32
Q

What types of coils and folds are there in a secondary structure?

A

Alpha helix -spiral
Beta pleated- side by side
Loops- parts of the protein that aren’t alpha helix or beta pleated

Biology (23 decks)

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