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B1 deck Flashcards

1
Q

How many covalent bonds can carbon form?

A

4

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2
Q

What is the shape of a carbon atom covalently bonded to four hydrogen atoms?

A

tetrahedral, with bond angles of approximately 109.5 degrees between each hydrogen atom.

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3
Q

What other atoms are typically included in organic molecules?

A

In addition to carbon and hydrogen, organic molecules commonly contain oxygen, nitrogen, sulfur, and phosphorus.

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4
Q

Define monomer.

A

A monomer is a small, simple molecule that can bind to other similar molecules to form a polymer.

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5
Q

Define polymer.

A

A polymer is a large molecule composed of monomers connected by covalent bonds.

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6
Q

What molecule is removed during a condensation reaction

A

a water molecule (H₂O) is removed as two monomers are joined together.

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7
Q

Diagram a condensation reaction between two monosaccharides.

A

B.1.1.2 (4)

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8
Q

What is a glycosidic bond?

A

covalent bond that links a carbohydrate (sugar) molecule to another molecule

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9
Q

What is the difference between alpha glucose and beta glucose?

A

Alpha glucose: The hydroxyl group on carbon 1 is positioned below the plane of the ring.
Beta glucose: The hydroxyl group on carbon 1 is positioned above the plane of the ring.

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10
Q

What is a hydrolysis reaction?

A

chemical process in which a water molecule is used to break the bonds between monomers in a polymer.

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11
Q

Diagram a hydrolysis reaction of a disaccharide.

A

B1.1.3 (2)

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12
Q

Draw a ribose and a glucose molecule.

A

b1.1.4 (1)

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13
Q

List 3 uses of glucose in plants and/or animals

A

Energy for cells (ATP).
Storage as starch or glycogen.
Building other molecules like cellulose.

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14
Q

What is the main energy storage molecule in plants and in animals?

A

Plants: Starch.
Animals: Glycogen.

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15
Q

What are the two types of starch?

A

Amylose (unbranched) and amylopectin (branched).

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16
Q

How do the two types of starch differ in structure?

A

Amylose: Unbranched, forms a helical structure, made of α-1,4 glycosidic bonds.
Amylopectin: Branched, has both α-1,4 and α-1,6 glycosidic bonds, making it more compact and easier to break down.

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17
Q

How is glycogen structured?

A

Glycogen is highly branched and made of α-glucose linked by α-1,4 glycosidic bonds, with branches formed by α-1,6 glycosidic bonds every 8–12 glucose units.

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18
Q

Which of the starch molecules is glycogen most similar to?

A

Amylopectin.

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19
Q

What is the molecular structure of cellulose?

A

Long chains of beta-glucose linked by hydrogen bonds.

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20
Q

What is cellulose used for in plant cells?

A

Provides structural support in cell walls.

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21
Q

What is a glycoprotein?

A

A protein with carbohydrate chains attached.

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22
Q

How are glycoproteins used in the ABO blood groups in humans?

A

They determine blood type based on specific sugars on red blood cells.

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23
Q

What are three classes of commonly occurring lipids?

A

Triglycerides (fats and oils)
Phospholipids
Steroids

24
Q

Draw a triglyceride

A

b1.1.9 (1)

25
How is a phospholipid different from a triglyceride?
A phospholipid has two fatty acids and a phosphate group instead of three fatty acids.
26
How are saturated and unsaturated fatty acids different?
Saturated: No double bonds, solid at room temp. Unsaturated: Has double bonds, liquid at room temp.
27
What is the difference between a cis unsaturated fatty acid and a trans unsaturated fatty acid?
Cis: Hydrogen atoms on the same side of the double bond (bent shape). Trans: Hydrogen atoms on opposite sides (straight shape).
28
Draw a cis and a trans arrangement around a double bond.
B1.1.10 (3)
29
How does saturation affect the physical properties of the lipid?
More saturated = solid (e.g., butter). More unsaturated = liquid (e.g., olive oil).
30
Adipose tissue is your fat storage tissue. What is the function of adipose tissue?
Stores energy and provides insulation.
31
Your cell membranes are made of a phospholipid bilayer. Draw a diagram showing the arrangement of phospholipids in the bilayer.
B1.1.12 (1)
32
Why do the phospholipids arrange in the way they do in the bilayer?
Hydrophilic (water-loving) heads face outward toward water (extracellular fluid and cytoplasm). Hydrophobic (water-fearing) tails face inward, away from water, creating a barrier that controls substance movement.
33
What is the basic structure of a steroid molecule?
B1.1.13 (1)
34
Why can steroids pass through the phospholipid bilayer?
They are non-polar and dissolve in lipids.
35
Draw and label a generalized structure of an amino acid.
B1.2.1 (1)
36
Draw a condensation reaction forming a dipeptide from two amino acids.
B1.2.2 (1)
37
What is the difference between an essential amino acid and a non-essential amino acid?
Essential: Must come from diet. Non-essential: Body can synthesize.
38
How many essential amino acids do humans have? Is this the same for all animals?
9 essential. Different for other animals.
39
State that with 20 different amino acids that can be put together in any order in any length, the possible variety of polypeptides is infinite.
20 amino acids can be combined in any order and length.
40
What is denaturation?
Loss of protein shape and function.
41
How do heat and pH cause denaturation?
They break bonds maintaining protein structure.
42
What 5 groups can the R-groups of amino acids be classified into?
Non-polar Polar Acidic (- charge) Basic (+ charge) Special cases (e.g., cysteine forms disulfide bonds)
43
What are the 4 levels of protein complexity?
Primary: Amino acid sequence. Secondary: Folding into helices or sheets. Tertiary: 3D shape. Quaternary: Multiple polypeptides together.
44
Describe what primary protein structure is.
the specific sequence of amino acids in a polypeptide chain, held together by peptide bonds. It determines the final shape and function of the protein.
45
What type of bond is most important in primary structure?
Peptide bonds.
46
Describe what secondary protein structure is.
Coiling (alpha-helix) or folding (beta-sheet) of the polypeptide chain.
47
What type of bond is most important in secondary structure?
Hydrogen bonds
48
Describe what an alpha-helix and a beta-pleated sheet are.
Alpha-helix: A coiled, spiral-shaped structure stabilized by hydrogen bonds between every fourth amino acid. Beta-pleated sheet: A folded, sheet-like structure formed when polypeptide chains lie parallel or antiparallel, held together by hydrogen bonds.
49
Describe what tertiary protein structure is.
3D shape of a polypeptide.
50
List the types of bonds involved in tertiary structure from strongest to weakest.
Disulfide bonds > Ionic bonds > Hydrogen bonds > Hydrophobic interactions.
51
How will polar and non-polar R-groups rotate in a protein due to the aqueous environment in a body?
Polar R-groups face outside (towards water). Non-polar R-groups stay inside (away from water).
52
What is the difference between conjugated and non-conjugated proteins?
Conjugated: Have a non-protein part (e.g., hemoglobin). Non-conjugated: Only amino acids.
53
Do all proteins have a quaternary structure? Explain.
No, only those with multiple polypeptides.
54
Describe what a globular and a fibrous protein are.
Globular: spherical, soluble (e.g., enzymes). Fibrous: Long, strong, insulable (e.g., collagen).
55
How do the functions of globular and fibrous proteins relate to their structure?
Globular: Enzymes, transport, signaling. Fibrous: Strength and support.

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