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AP Biology > Macromolecules > Flashcards

Macromolecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Structure v.s Function

A

Structure: Appearance, composition, location (relative and absolute), ect.
Function: Process, what something does.

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2
Q

Monomers

A

Repeating subunits that covalently bond together to form polymers

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3
Q

Polymers

A

Long chains of monomers bonded together covalently
- These chains are formed and broken apart in reactions involving water

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4
Q

Dehydration synthesis

A

Removal of water to bond smaller molecules together into larger molecules

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5
Q

Hydrolysis

A

Addition of water to break apart large molecules into smaller molecules

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6
Q

Carbohydrates

A

A type of macromolecule used for short-term energy. They are between cells for communication.

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7
Q

Monosaccharides

A

A monomer of larger carbohydrates
ex. glucose, fructose, ribose

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8
Q

Disaccharides

A

Two monosaccharides bonded together
ex. sucrose, lactose

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9
Q

Oligosaccharides

A

3-10 monosaccharides bonded together

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10
Q

Polysaccharides

A

Thousands of monosaccharides bonded together
ex. cellulose, starch, chitin, glycogen

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11
Q

Lipids (Macromolecule)

A

Another type of macromolecule, used for long-term energy storage. Deals with hormones and cushion/insulation.
- Not true polymers
- All are hydrophobic
- Van der Waals forces keep the molecules together
- Triglycerides, phospholipids, and cholesterol

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12
Q

Cholesterol

A

Only found in animal cells (similar to a cell wall function in a plant). 4 rings and a carbon chain

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13
Q

Triglycerides

A

The fat that you eat and store in your body. 1 glycerol and 3 fatty acids.

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14
Q

Saturated v.s unsaturated fatty acids

A

Saturated fatty acids have chains of carbons and hydrogen in which each carbon is bonded to at least 2 hydrogens. Unsaturated fatty acids do not. There may be a double bond between carbons, but that means it does not have as many hydrogen atoms as possible in that chain.

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15
Q

Nucleic acids

A

Store, transmit, and help express hereditary information. Codes for and helps build polypeptide chain (proteins)

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16
Q

DNA

A

Deoxyribonucleic acid

17
Q

RNA

A

Ribonucleic acid

18
Q

Protein function

A

Structure (hair, skin, nails, feathers, horns, ect.), communication, movement, transport, catalyst (enzymes), defense (antibodies).

19
Q

amino acids

A

Have a central C bonded to a carboxyl group, an amino group, a H atom, an R group (a variable group attached to the molecule)

Made up of C, H, N, O, and S atoms

20
Q

Protein Conformation: Primary structure

A

Sequence of covalently bonded amino acids between carboxyl and amine groups that form polypeptide chains
- Bonds: covalent

21
Q

Protein Conformation: Secondary structure

A

The folded regions of the polypeptide chain forming alpha helices and beta pleated sheets
- Bonds: hydrogen

22
Q

Protein Conformation: Tertiary structure

A

The 3D shape formed when the whole polypeptide chain is bent and folded upon itself
- Due to hydrophobic regions and disulfide bonds (bonds specific to proteins)
- Bonds: Covalent, hydrogen, ionic, van der waals

23
Q

Protein Conformation: Quaternary structure

A

Two or more polypeptide chains bound together to form large, complex protein.
- Not all proteins have quaternary structure
- Bonds: hydrogen, ionic, covalent/disulfide bridges, van der Waals

24
Q

Catalyst

A

A substance that speeds up a reaction without permanently being changed by the reaction.

25
Q

Enzymes

A

Biological catalysts that are highly specific to one reaction
- For our purposes, all are proteins
- Enzymes typically end in -ase

26
Q

Substrate

A

The substance on which an enzyme acts

27
Q

Active Site

A

The place on the enzyme in which the substrate(s) bond
- usually a hydrogen bond, an electrostatic attraction, or a temporary covalent bond

28
Q

Coenzyme/Cofactor

A

A vitamin or metal ion that helps an enzyme function

29
Q

Denature/Denaturation

A

When factors such as pH and temperature disrupt electrostatic attractions or bonds in the secondary or tertiary levels holding protein in its correct configuration
- May be permanent or temporary

30
Q

How do environmental conditions affect chemical reaction rate and enzyme functions?

A

Chemical reaction rates are highly dependent on environmental conditions
- Enzymes are optimized to function in specific conditions, and extremes could cause them to denature (they are proteins too)
- Organisms maintain homeostasis to allow these enzymes to function properly so you can get the nutrients you need in time to keep you alive

31
Q

How do enzymes work?

A

Enzymes are proteins that speed up reactions in living organisms, They bond to the substrate(s) and lower the activation energy by changing substrate orientation, stretching bonds, or creating a temporary charge change.

32
Q

What is the structure of Triglycerides?

A

One glycerol bonded to three fatty acid chains

33
Q

A DNA nucleotide containing adenine will hydrogen bond with a DNA nucleotide containing what? An RNA nucleotide?

A

DNA: Thymine
RNA: Uracil

34
Q

The breakdown of ethanol into acetaldehyde is facilitated by alcohol dehydrogenase with Zinc ions. Identify each component in this scenario (Product, substrate, enzyme, cofactor)

A

Product: Acetaldehyde
Substrate: Ethanol
Enzyme: Alcohol dehydrogenase
Cofactor: Zinc Ions

35
Q

Is Carbon Dioxide an organic molecule?

A

No, It does not contain carbon bonded to hydrogen

36
Q

What are the monomers for nucleic acids?

A

Nucleotides

37
Q

What are the elements found in carbohydrates? Lipids? Nucleic acids? Proteins?

A

Carbohydrates: Carbon, Hydrogen, Oxygen (CHO)
- 1:2:1 ratio
Lipids: Carbon, Hydrogen, Oxygen (CHO)
Nucleic acids: Carbon, Hydrogen, Oxygen, Nitrogen, Phosphorus (CHONP)
Proteins: Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur (CHONS)

AP Biology (10 decks)

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